{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T12:41:48Z","timestamp":1791895308219,"version":"4.3.4"},"reference-count":33,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5511","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2001,3,16]]},"abstract":"<jats:p>\n            <jats:italic>Caenorhabditis elegans<\/jats:italic>\n            oocytes, like those of most animals, arrest during meiotic prophase. Sperm promote the resumption of meiosis (maturation) and contraction of smooth muscle\u2013like gonadal sheath cells, which are required for ovulation. We show that the major sperm cytoskeletal protein (MSP) is a bipartite signal for oocyte maturation and sheath contraction. MSP also functions in sperm locomotion, playing a role analogous to actin. Thus, during evolution, MSP has acquired extracellular signaling and intracellular cytoskeletal functions for reproduction. Proteins with MSP-like domains are found in plants, fungi, and other animals, suggesting that related signaling functions may exist in other phyla.\n          <\/jats:p>","DOI":"10.1126\/science.1057586","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T09:47:44Z","timestamp":1027763264000},"page":"2144-2147","source":"Crossref","is-referenced-by-count":395,"title":["A Sperm Cytoskeletal Protein That Signals Oocyte Meiotic Maturation and Ovulation"],"prefix":"10.1126","volume":"291","author":[{"given":"Michael A.","family":"Miller","sequence":"first","affiliation":[{"name":"Department of Cell Biology,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Viet Q.","family":"Nguyen","sequence":"additional","affiliation":[{"name":"Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min-Ho","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary","family":"Kosinski","sequence":"additional","affiliation":[{"name":"Department of Cell Biology,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tim","family":"Schedl","sequence":"additional","affiliation":[{"name":"Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard M.","family":"Caprioli","sequence":"additional","affiliation":[{"name":"Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Greenstein","sequence":"additional","affiliation":[{"name":"Department of Cell Biology,"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1006\/dbio.1998.9109"},{"key":"e_1_3_1_3_2","unstructured":"To prepare SCM purified sperm (23) were incubated in M9 buffer (\u223c5 \u00d7 10 7 sperm per milliliter) for 1 to 16 hours at 20\u00b0C. Sperm were removed by centrifugation and filtration through a 0.22-\u03bcm cellulose acetate filter. After microinjection (\u223c50 pl) oocyte maturation and sheath cell contraction rates were monitored by time-lapse video microscopy (1) for 70 min."},{"key":"e_1_3_1_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/genetics\/119.1.43"},{"key":"e_1_3_1_5_2","unstructured":"Web movies 1 through 4 and Web fig. 1 are available at Science Online at www.sciencemag.org\/cgi\/content\/full\/291\/5511\/2144\/DC1."},{"key":"e_1_3_1_6_2","unstructured":"SCM or sperm lysates prepared by vortexing with glass beads were fractionated on C 4 and C 18 columns (Vydac Hesperia CA) using an acetonitrile gradient (0 to 100%) mobile phase containing 0.1% trifluoroacetic acid. Absorbance peaks (214 nm) were collected manually dialyzed against M9 and bioassayed."},{"key":"e_1_3_1_7_2","unstructured":"Active fractions were analyzed by MALDI-TOF mass spectrometry. Post source decay mass spectrometry (29) of a 1960-dalton peptide generated by tryptic digestion of the active fraction yielded the sequence IVFNAPYDDKHTYHIK (30) matching MSP."},{"key":"e_1_3_1_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(88)90374-9"},{"key":"e_1_3_1_9_2","unstructured":"M. Miller V. Nguyen R. Caprioli D. Greenstein unpublished data."},{"key":"e_1_3_1_10_2","unstructured":"His-tagged MSP-77 MSP-38 and MSP(1 to 106) were purified under native conditions by Ni\u2013nitrilotriacetic acid (Ni-NTA) (Qiagen Valencia CA) affinity chromatography (>99% pure by SDS-PAGE and MALDI-TOF). MSP concentrations were determined by amino acid hydrolysis SDS-PAGE and spectrophotometrically using \u03b5 (275 nm) = 3.29 \u00d7 10 4 M \u22121 cm \u22121 ."},{"key":"e_1_3_1_11_2","unstructured":"Antibodies to MSP (23) or EMB-30 control antibodies were injected (\u223c40 \u03bcg\/ml) into wild-type adult hermaphrodites (24 hours post-L4 at 20\u00b0C) which were then cultured individually with food for 3 hours. Total ovulations were determined (1) and oocyte maturation was analyzed by time-lapse video microscopy. A two-sample t test was used to assess statistical significance."},{"key":"e_1_3_1_12_2","doi-asserted-by":"crossref","unstructured":"K. L. Hill S. W. L'Hernault Dev. Biol. 232 105 (2001).","DOI":"10.1006\/dbio.2000.0136"},{"key":"e_1_3_1_13_2","unstructured":"The COOH-terminal MSP peptide (REWFQGDGMVRRKNLPIEYNP) (30) was prepared by solid-phase synthesis and purified by HPLC."},{"key":"e_1_3_1_14_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1521-1878(199910)21:10<833::AID-BIES5>3.0.CO;2-P"},{"key":"e_1_3_1_15_2","unstructured":"Diphosphorylated MPK-1 was detected using indirect immunofluorescence with the antibody MAPK-YT (31) (Sigma). Dissected and fixed (3% paraformaldehyde) gonads were stained 40 min post MSP injection."},{"key":"e_1_3_1_16_2","doi-asserted-by":"publisher","DOI":"10.1093\/genetics\/150.1.103"},{"key":"e_1_3_1_17_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1996.0575"},{"key":"e_1_3_1_18_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.7667638"},{"key":"e_1_3_1_19_2","doi-asserted-by":"crossref","unstructured":"L. Soussan et al. J. Cell Biol. 146 301 (1999).","DOI":"10.1083\/jcb.146.2.301"},{"key":"e_1_3_1_20_2","doi-asserted-by":"crossref","unstructured":"J. Ramalho-Santos et al. Dev. Biol. 223 54 (2000).","DOI":"10.1006\/dbio.2000.9745"},{"key":"e_1_3_1_21_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.38.24355"},{"key":"e_1_3_1_22_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.281.5385.1995"},{"key":"e_1_3_1_23_2","unstructured":"S. W. L'Hernault in C. elegans II D. L. Riddle T. Blumenthal B. J. Meyer J. R. Priess R. Eds. (Cold Spring Harbor Laboratory Press Cold Spring Harbor NY 1997) pp. 271\u2013294."},{"key":"e_1_3_1_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/0012-1606(81)90398-5"},{"key":"e_1_3_1_25_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.149.1.7"},{"key":"e_1_3_1_26_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.92.1.121"},{"key":"e_1_3_1_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80997-6"},{"key":"e_1_3_1_28_2","unstructured":"S. W. L'Hernault"},{"key":"e_1_3_1_28_3","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.119.1.55"},{"key":"e_1_3_1_29_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1998.1793"},{"key":"e_1_3_1_30_2","doi-asserted-by":"publisher","DOI":"10.1002\/rcm.1290071010"},{"key":"e_1_3_1_31_2","unstructured":"Single-letter abbreviations for the amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; and Y Tyr."},{"key":"e_1_3_1_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(97)00442-0"},{"key":"e_1_3_1_33_2","unstructured":"We thank S. Ward for providing antibodies and Y. Kohara for expressed sequence tag clones. Some strains used in this study were provided by the Caenorhabditis Genetics Center which is supported by NIH. We thank D. Bridge C. Desai B. Hogan D. Miller and R. Steele for helpful discussions and review of the manuscript. We thank E. Mitchell for digital video editing. M.A.M. and M.K. were supported by NIH training grants HD07043 and CA09592. Supported by grants from NIH (GM57173 to D.G. GM58008 to R.M.C. and HD25614 to T.S.)."}],"container-title":["Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/science.1057586","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T22:57:21Z","timestamp":1704841041000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/science.1057586"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,3,16]]},"references-count":33,"journal-issue":{"issue":"5511","published-print":{"date-parts":[[2001,3,16]]}},"alternative-id":["10.1126\/science.1057586"],"URL":"https:\/\/doi.org\/10.1126\/science.1057586","relation":{},"ISSN":["0036-8075","1095-9203"],"issn-type":[{"value":"0036-8075","type":"print"},{"value":"1095-9203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,3,16]]}}}