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Major NDDs include Alzheimer\u2019s disease, Parkinson\u2019s disease, amyotrophic lateral sclerosis, Huntington\u2019s disease, multiple sclerosis, and stroke. Although each disorder exhibits distinct genetic backgrounds and pathological protein aggregates, they share common pathogenic mechanisms, including chronic neuroinflammation, impaired autophagy and mitophagy, disrupted proteostasis, telomere instability, and epigenetic alterations. A hallmark feature across NDDs is the accumulation of misfolded proteins, leading to synaptic dysfunction and neuronal degeneration. Small ubiquitin-like modifiers (SUMOs) are a family of \u223c100 amino acid proteins, including SUMO1 and the closely related SUMO2\/3 isoforms. SUMOylation is a dynamic posttranslational modification that regulates protein function through the covalent attachment or removal of SUMO moieties. This reversible process is mediated by SUMO-specific E1 activating, E2 conjugating, and E3 ligating enzymes and is counterbalanced by SUMO\/Sentrin-specific proteases. The SUMOylation status of target proteins depends on the tightly controlled balance between conjugation and deconjugation systems. Acting as a molecular switch, SUMOylation modulates diverse cellular processes such as DNA damage repair, RNA metabolism, transcriptional regulation, and protein quality control, all of which are essential for maintaining cellular homeostasis. Accumulating evidence links dysregulated SUMOylation to the pathogenesis of multiple neurological disorders, including polyglutamine and synucleinopathies. SUMOylation influences neuroinflammation, oxidative stress, protein aggregation, neuroangiogenesis, ischemic injury, and demyelination. This review highlights recent advances in understanding the role of SUMOylation in NDDs and explores its potential as a promising therapeutic target.<\/jats:p>","DOI":"10.1177\/10445498261444640","type":"journal-article","created":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T06:50:53Z","timestamp":1778223053000},"page":"299-316","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":1,"title":["SUMOylation in Neural Health and Disease: From Cellular Homeostasis to Neurodegeneration"],"prefix":"10.1177","volume":"45","author":[{"given":"Ghaleb","family":"Oriquat","sequence":"first","affiliation":[{"name":"Faculty of Allied Medical Sciences, Hourani Center for Applied Scientific Research, Al-Ahliyya Amman University, Amman, Jordan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ihsan K.","family":"Jasim","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, College of Pharmacy, Al-Turath University, Baghdad, Iraq."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tushar B.","family":"Gajjar","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, Faculty of Pharmacy, Gokul Global University, Sidhpur, India."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malathi","family":"Hanumanthayya","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Genetics, School of Sciences, JAIN (Deemed to be University), Bangalore, India."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Israa","family":"Abdulhameed Ahmad","sequence":"additional","affiliation":[{"name":"Department of Anesthesia Techniques, Health and Medical Techniques College, Alnoor University, Mosul, Iraq."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gunjan","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, Sharda School of Pharmacy, Sharda University, Greater Noida, India."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laxmidhar","family":"Maharana","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Siksha \u2018O\u2019 Anusandhan (Deemed to be University), Bhubaneswar, India."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-1232-6088","authenticated-orcid":false,"given":"Neeraj","family":"Bainsal","sequence":"additional","affiliation":[{"name":"University Institute of Pharma Sciences, Chandigarh University, Mohali, India."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2026,5,7]]},"reference":[{"key":"e_1_3_3_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi501512m"},{"key":"e_1_3_3_3_1","doi-asserted-by":"publisher","DOI":"10.1161\/STROKEAHA.122.040578"},{"key":"e_1_3_3_4_1","doi-asserted-by":"publisher","DOI":"10.1097\/00001756-200008030-00029"},{"key":"e_1_3_3_5_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.e04-07-0589"},{"key":"e_1_3_3_6_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1800498115"},{"key":"e_1_3_3_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.106955"},{"issue":"5","key":"e_1_3_3_8_1","first-page":"971","article-title":"PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia","volume":"13","author":"Boddy MN","year":"1996","unstructured":"Boddy MN, , Howe K, , Etkin LD, et al. 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