{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T11:10:51Z","timestamp":1780571451743,"version":"3.54.1"},"reference-count":72,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,1,15]],"date-time":"2025-01-15T00:00:00Z","timestamp":1736899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,1,15]],"date-time":"2025-01-15T00:00:00Z","timestamp":1736899200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"the Special Supporting Program Project for the Research Institutions of Zhejiang Province","award":["C11920D-04"],"award-info":[{"award-number":["C11920D-04"]}]},{"DOI":"10.13039\/501100004731","name":"Natural Science Foundation of Zhejiang Province","doi-asserted-by":"publisher","award":["LY22H040011"],"award-info":[{"award-number":["LY22H040011"]}],"id":[{"id":"10.13039\/501100004731","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100013115","name":"Zhejiang Provincial Program for the Cultivation of High-Level Innovative Health Talents","doi-asserted-by":"publisher","award":["The Year 2018"],"award-info":[{"award-number":["The Year 2018"]}],"id":[{"id":"10.13039\/501100013115","id-type":"DOI","asserted-by":"publisher"}]},{"name":"the Clinical&Basic Joint Research Project of ZJPPH","award":["C-2023-YXLH11"],"award-info":[{"award-number":["C-2023-YXLH11"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biol Res"],"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:sec>\n            <jats:title>Background<\/jats:title>\n            <jats:p>Protein palmitoylation, a critical posttranslational modification, plays an indispensable role in various cellular processes, including the regulation of protein stability, mediation of membrane fusion, facilitation of intracellular protein trafficking, and participation in cellular signaling pathways. It is also implicated in the pathogenesis of diseases, such as cancer, neurological disorders, inflammation, metabolic disorders, infections, and neurodegenerative diseases. However, its regulatory effects on sperm physiology, particularly motility, remain unclear. This study aimed to elucidate the mechanism by which protein palmitoylation governs sperm motility.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Methods<\/jats:title>\n            <jats:p>Protein palmitoylation in situ in mouse sperm was observed using innovative click chemistry. Sperm motility and motion parameters were evaluated using a computer-assisted sperm analyzer (CASA) after treatment with 2-bromopalmitic acid (2BP), a specific inhibitor of protein palmitoylation. Protein palmitoylation levels were confirmed by the acyl-biotin exchange (ABE) method. The interplay between protein palmitoylation, protein tyrosine phosphorylation, and intracellular calcium was investigated using Western blotting, ABE method, and fluorescent probes. The regulation of reactive oxygen species was also examined using fluorescent probes.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>Localized patterns and dynamics of protein palmitoylation in distinct sperm regions were revealed, including the midpiece, post-acrosomal region, acrosome, and head. Alterations in protein palmitoylation in sperm were observed under in vitro physiological conditions. Treatment with 2BP significantly affected sperm motility and motion parameters. The study revealed interactions between protein palmitoylation, including heat shock protein 90, and protein kinase A\/protein kinase C-associated protein tyrosine phosphorylation and intracellular calcium. Additionally, protein palmitoylation was found to be involved in reactive oxygen species regulation.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>Protein palmitoylation regulates sperm motility through calcium signaling, protein tyrosine phosphorylation, and reactive oxygen species. This study revealed the characteristics of protein palmitoylation in sperm and its role in regulating sperm motility, thereby providing novel insights into the causes of asthenozoospermia associated with sperm motility in humans.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/s40659-024-00580-4","type":"journal-article","created":{"date-parts":[[2025,1,15]],"date-time":"2025-01-15T03:37:52Z","timestamp":1736912272000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Protein palmitoylation is involved in regulating mouse sperm motility via the signals of calcium, protein tyrosine phosphorylation and reactive oxygen species"],"prefix":"10.1186","volume":"58","author":[{"given":"Yuping","family":"Xiong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chenchen","family":"Yi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haixia","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ya","family":"Ni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yamei","family":"Xue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0678-1122","authenticated-orcid":false,"given":"Kun","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,1,15]]},"reference":[{"key":"580_CR1","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1038\/nrm2084","volume":"8","author":"ME Linder","year":"2007","unstructured":"Linder ME, Deschenes RJ. Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol. 2007;8:74\u201384.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"580_CR2","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.tibs.2011.01.003","volume":"36","author":"J Greaves","year":"2011","unstructured":"Greaves J, Chamberlain LH. DHHC palmitoyl transferases: substrate interactions and (patho)physiology. Trends Biochem Sci. 2011;36:245\u201353.","journal-title":"Trends Biochem Sci"},{"key":"580_CR3","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/j.plipres.2009.02.001","volume":"48","author":"T Iwanaga","year":"2009","unstructured":"Iwanaga T, Tsutsumi R, Noritake J, Fukata Y, Fukata M. Dynamic protein palmitoylation in cellular signaling. Prog Lipid Res. 2009;48:117\u201327.","journal-title":"Prog Lipid Res"},{"key":"580_CR4","doi-asserted-by":"publisher","first-page":"e46666","DOI":"10.15252\/embr.201846666","volume":"19","author":"PJ Ko","year":"2018","unstructured":"Ko PJ, Dixon SJ. Protein palmitoylation and cancer. EMBO Rep. 2018;19:e46666.","journal-title":"EMBO Rep"},{"key":"580_CR5","doi-asserted-by":"publisher","first-page":"4223","DOI":"10.7150\/ijbs.64046","volume":"17","author":"M Qu","year":"2021","unstructured":"Qu M, Zhou X, Wang X, Li H. Lipid-induced S-palmitoylation as a Vital Regulator of Cell Signaling and Disease Development. Int J Biol Sci. 2021;17:4223\u201337.","journal-title":"Int J Biol Sci"},{"key":"580_CR6","first-page":"298","volume":"69","author":"R Li","year":"2017","unstructured":"Li R, Li K, Yang Y, Sun PB, Chen AJ, Ni Y. Palmitoylation of heat shock protein 90 in mouse sperm. Sheng Li Xue Bao. 2017;69:298\u2013304.","journal-title":"Sheng Li Xue Bao"},{"key":"580_CR7","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1530\/REP-20-0423","volume":"161","author":"D Dong","year":"2021","unstructured":"Dong D, Yang J, Chen Y, Peng G, Cao H, Gao H, et al. Palmitoylated GLB1L4 transfers via exosomes to maintain sperm function in rat epididymis. Reproduction. 2021;161:159\u201372.","journal-title":"Reproduction"},{"key":"580_CR8","doi-asserted-by":"publisher","first-page":"2299","DOI":"10.1007\/s43032-022-00919-w","volume":"29","author":"J Gao","year":"2022","unstructured":"Gao J, Li W, Zhang Z, Gao W, Kong E. Proteome-wide identification of palmitoylated proteins in mouse testis. Reprod Sci. 2022;29:2299\u2013309.","journal-title":"Reprod Sci"},{"key":"580_CR9","doi-asserted-by":"publisher","first-page":"102380","DOI":"10.1016\/j.redox.2022.102380","volume":"54","author":"X Ge","year":"2022","unstructured":"Ge X, He Z, Cao C, Xue T, Jing J, Ma R, et al. Protein palmitoylation-mediated palmitic acid sensing causes blood-testis barrier damage via inducing ER stress. Redox Biol. 2022;54:102380.","journal-title":"Redox Biol"},{"key":"580_CR10","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1038\/s41556-021-00832-5","volume":"24","author":"L Thomas","year":"2022","unstructured":"Thomas L, Seydoux G. Sperm granules mediate epigenetic inheritance. Nat Cell Biol. 2022;24:129\u201330.","journal-title":"Nat Cell Biol"},{"key":"580_CR11","doi-asserted-by":"crossref","unstructured":"Wang S, Qiao H, Wang P, Wang Y, Qin D. ZDHHC19 is dispensable for spermatogenesis, but is essential for sperm functions in mice. Int J Mol Sci. 2021;22:8894.","DOI":"10.3390\/ijms22168894"},{"key":"580_CR12","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1093\/biolre\/ioab224","volume":"106","author":"Y Wu","year":"2022","unstructured":"Wu Y, Zhang X, Zhang X, Liu S, Zhang J, Sun S, et al. ZDHHC19 localizes to the cell membrane of spermatids and is involved in spermatogenesisdagger. Biol Reprod. 2022;106:477\u201386.","journal-title":"Biol Reprod"},{"key":"580_CR13","doi-asserted-by":"publisher","first-page":"818","DOI":"10.1016\/j.tibs.2018.08.006","volume":"43","author":"Y Satouh","year":"2018","unstructured":"Satouh Y, Ikawa M. New insights into the molecular events of mammalian fertilization. Trends Biochem Sci. 2018;43:818\u201328.","journal-title":"Trends Biochem Sci"},{"key":"580_CR14","first-page":"2","volume":"96","author":"MJ Freitas","year":"2017","unstructured":"Freitas MJ, Vijayaraghavan S, Fardilha M. Signaling mechanisms in mammalian sperm motility. Biol Reprod. 2017;96:2\u201312.","journal-title":"Biol Reprod"},{"key":"580_CR15","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1016\/j.ceb.2020.01.015","volume":"63","author":"L Vyklicka","year":"2020","unstructured":"Vyklicka L, Lishko PV. Dissecting the signaling pathways involved in the function of sperm flagellum. Curr Opin Cell Biol. 2020;63:154\u201361.","journal-title":"Curr Opin Cell Biol"},{"key":"580_CR16","doi-asserted-by":"publisher","first-page":"e115841","DOI":"10.1371\/journal.pone.0115841","volume":"9","author":"K Li","year":"2014","unstructured":"Li K, Xue Y, Chen A, Jiang Y, Xie H, Shi Q, et al. Heat shock protein 90 has roles in intracellular calcium homeostasis, protein tyrosine phosphorylation regulation, and progesterone-responsive sperm function in human sperm. PLoS ONE. 2014;9:e115841.","journal-title":"PLoS ONE"},{"key":"580_CR17","doi-asserted-by":"publisher","first-page":"765","DOI":"10.1007\/s00441-012-1370-3","volume":"349","author":"J Signorelli","year":"2012","unstructured":"Signorelli J, Diaz ES, Morales P. Kinases, phosphatases and proteases during sperm capacitation. Cell Tissue Res. 2012;349:765\u201382.","journal-title":"Cell Tissue Res"},{"key":"580_CR18","doi-asserted-by":"publisher","first-page":"1305","DOI":"10.1152\/physrev.00028.2010","volume":"91","author":"A Darszon","year":"2011","unstructured":"Darszon A, Nishigaki T, Beltran C, Trevino CL. Calcium channels in the development, maturation, and function of spermatozoa. Physiol Rev. 2011;91:1305\u201355.","journal-title":"Physiol Rev"},{"key":"580_CR19","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1038\/ncb0307-235","volume":"9","author":"S Publicover","year":"2007","unstructured":"Publicover S, Harper CV, Barratt C. [Ca2+]i signalling in sperm\u2013making the most of what you\u2019ve got. Nat Cell Biol. 2007;9:235\u201342.","journal-title":"Nat Cell Biol"},{"key":"580_CR20","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.mce.2005.12.026","volume":"250","author":"RJ Aitken","year":"2006","unstructured":"Aitken RJ, Baker MA. Oxidative stress, sperm survival and fertility control. Mol Cell Endocrinol. 2006;250:66\u20139.","journal-title":"Mol Cell Endocrinol"},{"key":"580_CR21","doi-asserted-by":"publisher","first-page":"577","DOI":"10.1093\/biolre\/iox104","volume":"97","author":"C O\u2019Flaherty","year":"2017","unstructured":"O\u2019Flaherty C, Matsushita-Fournier D. Reactive oxygen species and protein modifications in spermatozoa. Biol Reprod. 2017;97:577\u201385.","journal-title":"Biol Reprod"},{"key":"580_CR22","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1093\/humupd\/dmn004","volume":"14","author":"K Tremellen","year":"2008","unstructured":"Tremellen K. Oxidative stress and male infertility\u2013a clinical perspective. Hum Reprod Update. 2008;14:243\u201358.","journal-title":"Hum Reprod Update"},{"key":"580_CR23","doi-asserted-by":"publisher","first-page":"e26044","DOI":"10.1371\/journal.pone.0026044","volume":"6","author":"PC Echeverria","year":"2011","unstructured":"Echeverria PC, Bernthaler A, Dupuis P, Mayer B, Picard D. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS ONE. 2011;6:e26044.","journal-title":"PLoS ONE"},{"key":"580_CR24","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1038\/nrm.2017.20","volume":"18","author":"FH Schopf","year":"2017","unstructured":"Schopf FH, Biebl MM, Buchner J. The HSP90 chaperone machinery. Nat Rev Mol Cell Biol. 2017;18:345\u201360.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"580_CR25","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1038\/nrm2918","volume":"11","author":"M Taipale","year":"2010","unstructured":"Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol. 2010;11:515\u201328.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"580_CR26","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1111\/andr.12862","volume":"9","author":"K Li","year":"2021","unstructured":"Li K, Sun P, Wang Y, Gao T, Zheng D, Liu A, et al. Hsp90 interacts with Cdc37, is phosphorylated by PKA\/PKC, and regulates src phosphorylation in human sperm capacitation. Andrology. 2021;9:185\u201395.","journal-title":"Andrology"},{"key":"580_CR27","doi-asserted-by":"publisher","first-page":"2847","DOI":"10.1007\/s43032-022-00862-w","volume":"29","author":"C Yi","year":"2022","unstructured":"Yi C, Ni Y, Sun P, Gao T, Li K. Differential size distribution and Estrogen Receptor Cargo of Oviductal Extracellular Vesicles at various stages of Estrous Cycle in mice. Reprod Sci. 2022;29:2847\u201358.","journal-title":"Reprod Sci"},{"key":"580_CR28","doi-asserted-by":"publisher","first-page":"11932","DOI":"10.1038\/ncomms11932","volume":"7","author":"K Mukai","year":"2016","unstructured":"Mukai K, Konno H, Akiba T, Uemura T, Waguri S, Kobayashi T, et al. Activation of STING requires palmitoylation at the Golgi. Nat Commun. 2016;7:11932.","journal-title":"Nat Commun"},{"key":"580_CR29","first-page":"737","volume":"6","author":"SJ Chmura","year":"2000","unstructured":"Chmura SJ, Dolan ME, Cha A, Mauceri HJ, Kufe DW, Weichselbaum RR. In vitro and in vivo activity of protein kinase C inhibitor chelerythrine chloride induces tumor cell toxicity and growth delay in vivo. Clin Cancer Res. 2000;6:737\u201342.","journal-title":"Clin Cancer Res"},{"key":"580_CR30","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s12276-019-0299-y","volume":"51","author":"JR Lee","year":"2019","unstructured":"Lee JR, Lee JY, Kim HJ, Hahn MJ, Kang JS, Cho H. The inhibition of chloride intracellular channel 1 enhances ca(2+) and reactive oxygen species signaling in A549 human lung cancer cells. Exp Mol Med. 2019;51:1\u201311.","journal-title":"Exp Mol Med"},{"key":"580_CR31","doi-asserted-by":"publisher","first-page":"1103","DOI":"10.1038\/sj.cdd.4400917","volume":"8","author":"F Philippoussis","year":"2001","unstructured":"Philippoussis F, Przybytkowski E, Fortin M, Arguin C, Pande SV, Steff AM, et al. Derivatives of monoglycerides as apoptotic agents in T-cells. Cell Death Differ. 2001;8:1103\u201312.","journal-title":"Cell Death Differ"},{"key":"580_CR32","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1016\/j.bcp.2012.08.028","volume":"84","author":"L Tucker-Kellogg","year":"2012","unstructured":"Tucker-Kellogg L, Shi Y, White JK, Pervaiz S. Reactive oxygen species (ROS) and sensitization to TRAIL-induced apoptosis, in bayesian network modelling of HeLa cell response to LY303511. Biochem Pharmacol. 2012;84:1307\u201317.","journal-title":"Biochem Pharmacol"},{"key":"580_CR33","doi-asserted-by":"publisher","first-page":"1207","DOI":"10.1095\/biolreprod.110.088989","volume":"84","author":"SG Goodson","year":"2011","unstructured":"Goodson SG, Zhang Z, Tsuruta JK, Wang W, O\u2019Brien DA. Classification of mouse sperm motility patterns using an automated multiclass support vector machines model. Biol Reprod. 2011;84:1207\u201315.","journal-title":"Biol Reprod"},{"key":"580_CR34","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1146\/annurev.biochem.73.011303.073954","volume":"73","author":"JE Smotrys","year":"2004","unstructured":"Smotrys JE, Linder ME. Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem. 2004;73:559\u201387.","journal-title":"Annu Rev Biochem"},{"key":"580_CR35","doi-asserted-by":"publisher","first-page":"7178","DOI":"10.1021\/acs.chemrev.0c01108","volume":"121","author":"KF Suazo","year":"2021","unstructured":"Suazo KF, Park KY, Distefano MD. A Not-So-Ancient grease history: click Chemistry and protein lipid modifications. Chem Rev. 2021;121:7178\u2013248.","journal-title":"Chem Rev"},{"key":"580_CR36","doi-asserted-by":"publisher","first-page":"e3001590","DOI":"10.1371\/journal.pbio.3001590","volume":"20","author":"EL Gorenberg","year":"2022","unstructured":"Gorenberg EL, Massaro Tieze S, Yucel B, Zhao HR, Chou V, Wirak GS, et al. Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function. PLoS Biol. 2022;20:e3001590.","journal-title":"PLoS Biol"},{"key":"580_CR37","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1002\/1878-0261.13308","volume":"17","author":"B Zhou","year":"2023","unstructured":"Zhou B, Hao Q, Liang Y, Kong E. Protein palmitoylation in cancer: molecular functions and therapeutic potential. Mol Oncol. 2023;17:3\u201326.","journal-title":"Mol Oncol"},{"key":"580_CR38","doi-asserted-by":"publisher","first-page":"4307","DOI":"10.1016\/0006-2952(87)90676-9","volume":"36","author":"S Abd El-Aleem","year":"1987","unstructured":"Abd El-Aleem S, Schulz H. Evaluation of inhibitors of fatty acid oxidation in rat myocytes. Biochem Pharmacol. 1987;36:4307\u201312.","journal-title":"Biochem Pharmacol"},{"key":"580_CR39","doi-asserted-by":"publisher","first-page":"e75232","DOI":"10.1371\/journal.pone.0075232","volume":"8","author":"MP Pedro","year":"2013","unstructured":"Pedro MP, Vilcaes AA, Tomatis VM, Oliveira RG, Gomez GA, Daniotti JL. 2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. PLoS ONE. 2013;8:e75232.","journal-title":"PLoS ONE"},{"key":"580_CR40","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1186\/s12860-018-0170-3","volume":"19","author":"CM Batista","year":"2018","unstructured":"Batista CM, Kessler RL, Eger I, Soares MJ. Treatment of Trypanosoma Cruzi with 2-bromopalmitate alters morphology, endocytosis, differentiation and infectivity. BMC Cell Biol. 2018;19:19.","journal-title":"BMC Cell Biol"},{"key":"580_CR41","doi-asserted-by":"publisher","first-page":"11796","DOI":"10.18632\/aging.206080","volume":"16","author":"A Krzystyniak","year":"2024","unstructured":"Krzystyniak A, Gluchowska A, Pytys A, Dudkowska M, Wojtowicz T, Targonska A, et al. 2-Bromopalmitate treatment attenuates senescence phenotype in human adult cells - possible role of palmitoylation. Aging. 2024;16:11796\u2013808.","journal-title":"Aging"},{"key":"580_CR42","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1194\/jlr.M800270-JLR200","volume":"50","author":"BC Jennings","year":"2009","unstructured":"Jennings BC, Nadolski MJ, Ling Y, Baker MB, Harrison ML, Deschenes RJ, et al. 2-Bromopalmitate and 2-(2-hydroxy-5-nitro-benzylidene)-benzo[b]thiophen-3-one inhibit DHHC-mediated palmitoylation in vitro. J Lipid Res. 2009;50:233\u201342.","journal-title":"J Lipid Res"},{"key":"580_CR43","doi-asserted-by":"publisher","first-page":"1625","DOI":"10.1111\/cmi.12601","volume":"18","author":"CS Hopp","year":"2016","unstructured":"Hopp CS, Balaban AE, Bushell ES, Billker O, Rayner JC, Sinnis P. Palmitoyl transferases have critical roles in the development of mosquito and liver stages of Plasmodium. Cell Microbiol. 2016;18:1625\u201341.","journal-title":"Cell Microbiol"},{"key":"580_CR44","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1016\/j.bpj.2019.08.018","volume":"118","author":"JJ Chen","year":"2020","unstructured":"Chen JJ, Marsden AN, Scott CA, Akimzhanov AM, Boehning D. DHHC5 mediates beta-adrenergic signaling in Cardiomyocytes by Targeting Galpha proteins. Biophys J. 2020;118:826\u201335.","journal-title":"Biophys J"},{"key":"580_CR45","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1186\/s12964-015-0105-y","volume":"13","author":"S Heiler","year":"2015","unstructured":"Heiler S, Mu W, Zoller M, Thuma F. The importance of claudin-7 palmitoylation on membrane subdomain localization and metastasis-promoting activities. Cell Commun Signal. 2015;13:29.","journal-title":"Cell Commun Signal"},{"key":"580_CR46","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1182\/blood-2014-04-571331","volume":"125","author":"X Lu","year":"2015","unstructured":"Lu X, Sicard R, Jiang X, Stockus JN, McNamara G, Abdulreda M, et al. HGAL localization to cell membrane regulates B-cell receptor signaling. Blood. 2015;125:649\u201357.","journal-title":"Blood"},{"key":"580_CR47","doi-asserted-by":"publisher","first-page":"100021","DOI":"10.1194\/jlr.RA120001190","volume":"62","author":"P Tripathi","year":"2021","unstructured":"Tripathi P, Zhu Z, Qin H, Elsherbini A, Crivelli SM, Roush E, et al. Palmitoylation of acetylated tubulin and association with ceramide-rich platforms is critical for ciliogenesis. J Lipid Res. 2021;62:100021.","journal-title":"J Lipid Res"},{"key":"580_CR48","doi-asserted-by":"crossref","unstructured":"Roy K, Marin EP. Lipid modifications in Cilia Biology. J Clin Med. 2019;8:921.","DOI":"10.3390\/jcm8070921"},{"key":"580_CR49","doi-asserted-by":"publisher","first-page":"2313","DOI":"10.1016\/j.devcel.2021.07.015","volume":"56","author":"Y Lei","year":"2021","unstructured":"Lei Y, Zhang X, Xu Q, Liu S, Li C, Jiang H, et al. Autophagic elimination of ribosomes during spermiogenesis provides energy for flagellar motility. Dev Cell. 2021;56:2313\u2013e287.","journal-title":"Dev Cell"},{"key":"580_CR50","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/B978-0-12-394305-7.00003-3","volume":"294","author":"A Konno","year":"2012","unstructured":"Konno A, Setou M, Ikegami K. Ciliary and flagellar structure and function\u2013their regulations by posttranslational modifications of axonemal tubulin. Int Rev Cell Mol Biol. 2012;294:133\u201370.","journal-title":"Int Rev Cell Mol Biol"},{"key":"580_CR51","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1016\/j.etap.2018.07.010","volume":"62","author":"S Huang","year":"2018","unstructured":"Huang S, Cao S, Zhou T, Kong L, Liang G. 4-tert-octylphenol injures motility and viability of human sperm by affecting cAMP-PKA\/PKC-tyrosine phosphorylation signals. Environ Toxicol Pharmacol. 2018;62:234\u201343.","journal-title":"Environ Toxicol Pharmacol"},{"key":"580_CR52","doi-asserted-by":"publisher","first-page":"398","DOI":"10.1017\/S0967199421000915","volume":"30","author":"A Loza-Huerta","year":"2022","unstructured":"Loza-Huerta A, Pacheco-Castillo H, Darszon A, Beltran C. Crosstalk between protein kinases a and C regulates sea urchin sperm motility. Zygote. 2022;30:398\u2013409.","journal-title":"Zygote"},{"key":"580_CR53","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1186\/1477-7827-2-75","volume":"2","author":"RK Naz","year":"2004","unstructured":"Naz RK, Rajesh PB. Role of tyrosine phosphorylation in sperm capacitation \/ acrosome reaction. Reprod Biol Endocrinol. 2004;2:75.","journal-title":"Reprod Biol Endocrinol"},{"key":"580_CR54","doi-asserted-by":"publisher","first-page":"2412","DOI":"10.1097\/CM9.0000000000001551","volume":"134","author":"YY Wang","year":"2021","unstructured":"Wang YY, Sun PB, Li K, Gao T, Zheng DW, Wu FP, et al. Protein kinases regulate hyperactivated motility of human sperm. Chin Med J (Engl). 2021;134:2412\u201314.","journal-title":"Chin Med J (Engl)"},{"key":"580_CR55","doi-asserted-by":"publisher","first-page":"102","DOI":"10.3324\/haematol.2018.191916","volume":"104","author":"Y Lu","year":"2019","unstructured":"Lu Y, Yan JS, Xia L, Qin K, Yin QQ, Xu HT, et al. 2-Bromopalmitate targets retinoic acid receptor alpha and overcomes all-trans retinoic acid resistance of acute promyelocytic leukemia. Haematologica. 2019;104:102\u201312.","journal-title":"Haematologica"},{"key":"580_CR56","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1038\/s41419-022-05235-4","volume":"13","author":"P Yan","year":"2022","unstructured":"Yan P, Liu H, Zhou T, Sun P, Wang Y, Wang X, et al. Crosstalk of Synapsin1 palmitoylation and phosphorylation controls the dynamicity of synaptic vesicles in neurons. Cell Death Dis. 2022;13:786.","journal-title":"Cell Death Dis"},{"key":"580_CR57","doi-asserted-by":"publisher","first-page":"29095","DOI":"10.1074\/jbc.M115.667055","volume":"290","author":"AE Moritz","year":"2015","unstructured":"Moritz AE, Rastedt DE, Stanislowski DJ, Shetty M, Smith MA, Vaughan RA, et al. Reciprocal phosphorylation and Palmitoylation Control Dopamine Transporter Kinetics. J Biol Chem. 2015;290:29095\u2013105.","journal-title":"J Biol Chem"},{"key":"580_CR58","doi-asserted-by":"publisher","first-page":"3284","DOI":"10.1091\/mbc.e13-12-0737","volume":"25","author":"A Gauthier-Kemper","year":"2014","unstructured":"Gauthier-Kemper A, Igaev M, Sundermann F, Janning D, Bruhmann J, Moschner K, et al. Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43. Mol Biol Cell. 2014;25:3284\u201399.","journal-title":"Mol Biol Cell"},{"key":"580_CR59","doi-asserted-by":"publisher","first-page":"1888","DOI":"10.1007\/s11426-011-4428-2","volume":"54","author":"X Guan","year":"2011","unstructured":"Guan X, Fierke CA. Understanding protein palmitoylation: biological significance and enzymology. Sci China Chem. 2011;54:1888\u201397.","journal-title":"Sci China Chem"},{"key":"580_CR60","doi-asserted-by":"publisher","first-page":"1156","DOI":"10.1136\/gutjnl-2023-330826","volume":"73","author":"L Bu","year":"2024","unstructured":"Bu L, Zhang Z, Chen J, Fan Y, Guo J, Su Y, et al. High-fat diet promotes liver tumorigenesis via palmitoylation and activation of AKT. Gut. 2024;73:1156\u201368.","journal-title":"Gut"},{"key":"580_CR61","doi-asserted-by":"publisher","first-page":"11953","DOI":"10.1021\/bi980565w","volume":"37","author":"DA Ford","year":"1998","unstructured":"Ford DA, Horner CC, Gross RW. Protein kinase C acylation by palmitoyl coenzyme a facilitates its translocation to membranes. Biochemistry. 1998;37:11953\u201361.","journal-title":"Biochemistry"},{"issue":"Pt 3","key":"580_CR62","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1042\/bj3030749","volume":"303","author":"M Koegl","year":"1994","unstructured":"Koegl M, Zlatkine P, Ley SC, Courtneidge SA, Magee AI. Palmitoylation of multiple src-family kinases at a homologous N-terminal motif. Biochem J. 1994;303(Pt 3):749\u201353.","journal-title":"Biochem J"},{"key":"580_CR63","doi-asserted-by":"publisher","first-page":"32161","DOI":"10.1074\/jbc.M112.386359","volume":"287","author":"X Zhou","year":"2012","unstructured":"Zhou X, Wulfsen I, Korth M, McClafferty H, Lukowski R, Shipston MJ, et al. Palmitoylation and membrane association of the stress axis regulated insert (STREX) controls BK channel regulation by protein kinase C. J Biol Chem. 2012;287:32161\u201371.","journal-title":"J Biol Chem"},{"key":"580_CR64","doi-asserted-by":"publisher","first-page":"102254","DOI":"10.1016\/j.ceca.2020.102254","volume":"91","author":"E Veseli","year":"2020","unstructured":"Veseli E, Soboloff J. Palmitoylation: a new mechanism for control of NCX1 function. Cell Calcium. 2020;91:102254.","journal-title":"Cell Calcium"},{"key":"580_CR65","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1530\/REP-14-0471","volume":"149","author":"RD Peralta-Arias","year":"2015","unstructured":"Peralta-Arias RD, Vivenes CY, Camejo MI, Pinero S, Proverbio T, Martinez E, et al. ATPases, ion exchangers and human sperm motility. Reproduction. 2015;149:475\u201384.","journal-title":"Reproduction"},{"key":"580_CR66","doi-asserted-by":"publisher","first-page":"3068","DOI":"10.1002\/jcp.25044","volume":"230","author":"JL Torres-Fuentes","year":"2015","unstructured":"Torres-Fuentes JL, Rios M, Moreno RD. Involvement of a P2X7 Receptor in the Acrosome Reaction Induced by ATP in Rat Spermatozoa. J Cell Physiol. 2015;230:3068\u201375.","journal-title":"J Cell Physiol"},{"key":"580_CR67","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1042\/BST20230818","volume":"52","author":"R Nere","year":"2024","unstructured":"Nere R, Kouba S, Carreras-Sureda A, Demaurex N. S-acylation of Ca2\u2009+\u2009transport proteins: molecular basis and functional consequences. Biochem Soc Trans. 2024;52:407\u201321.","journal-title":"Biochem Soc Trans"},{"key":"580_CR68","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1016\/j.bbamcr.2013.02.022","volume":"1833","author":"MG De Napoli","year":"2013","unstructured":"De Napoli MG, de Miguel N, Lebrun M, Moreno SN, Angel SO, Corvi MM. N-terminal palmitoylation is required for Toxoplasma Gondii HSP20 inner membrane complex localization. Biochim Biophys Acta. 2013;1833:1329\u201337.","journal-title":"Biochim Biophys Acta"},{"key":"580_CR69","doi-asserted-by":"publisher","first-page":"3249","DOI":"10.1128\/MCB.01354-09","volume":"30","author":"M Razandi","year":"2010","unstructured":"Razandi M, Pedram A, Levin ER. Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane. Mol Cell Biol. 2010;30:3249\u201361.","journal-title":"Mol Cell Biol"},{"key":"580_CR70","doi-asserted-by":"publisher","first-page":"112076","DOI":"10.1016\/j.mce.2023.112076","volume":"578","author":"S Zhao","year":"2023","unstructured":"Zhao S, Ma R, Jueraitetibaike K, Xu Y, Jing J, Tang T, et al. ZDHHC17 participates in the pathogenesis of polycystic ovary syndrome by affecting androgen conversion to estrogen in granulosa cells. Mol Cell Endocrinol. 2023;578:112076.","journal-title":"Mol Cell Endocrinol"},{"key":"580_CR71","doi-asserted-by":"publisher","first-page":"110953","DOI":"10.1016\/j.mce.2020.110953","volume":"516","author":"M Finkelstein","year":"2020","unstructured":"Finkelstein M, Etkovitz N, Breitbart H. Ca(2+) signaling in mammalian spermatozoa. Mol Cell Endocrinol. 2020;516:110953.","journal-title":"Mol Cell Endocrinol"},{"key":"580_CR72","doi-asserted-by":"publisher","first-page":"200118","DOI":"10.1098\/rsob.200118","volume":"10","author":"P Stein","year":"2020","unstructured":"Stein P, Savy V, Williams AM, Williams CJ. Modulators of calcium signalling at fertilization. Open Biol. 2020;10:200118.","journal-title":"Open Biol"}],"container-title":["Biological Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s40659-024-00580-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s40659-024-00580-4\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s40659-024-00580-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,1,15]],"date-time":"2025-01-15T04:34:24Z","timestamp":1736915664000},"score":1,"resource":{"primary":{"URL":"https:\/\/biolres.biomedcentral.com\/articles\/10.1186\/s40659-024-00580-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,15]]},"references-count":72,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["580"],"URL":"https:\/\/doi.org\/10.1186\/s40659-024-00580-4","relation":{},"ISSN":["0717-6287"],"issn-type":[{"value":"0717-6287","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,15]]},"assertion":[{"value":"6 September 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 December 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 January 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"All animal study procedures were approved by the local Laboratory Animal Welfare Ethics Committee.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"3"}}