Conserved ß-tubulin binding domain for the microtubule-associated motors underlying sperm motility and fast axonal transport Journal Article
| Authors: | Goldsmith, M.; Connolly, J. A.; Kumar, N.; Wu, J.; Yarbrough, L. R.; Vanderkooy, D. |
| Article Title: | Conserved ß-tubulin binding domain for the microtubule-associated motors underlying sperm motility and fast axonal transport |
| Abstract: | An antiserum against tubulin, NS20, has been previously shown to inhibit anterograde and retrograde axonal transport by 50% in vivo and in vitro. We report here that Protein A purified NS20 antibodies also attenuate sperm motility by 50% in demembranated sea urchin sperm. This inhibition is absorbed out by preincubating the NS20 antibodies with a biochemically purified porcine microtubule preparation, with recombinant Trypanosoma beta- (but not alpha-) tubulin and most specifically, with a 37 amino acid (a.a) synthetic peptide corresponding to a domain near (but not including) the porcine beta-tubulin C terminus. Furthermore, addition of this beta-tubulin peptide alone is sufficient to attenuate motility by 50% in demembranated sperm, indicating that this critical 37a.a. NS20 antigen is a motor binding domain. Together, the results suggest that at least two phenotypically distinct forms of microtubule-based motility, axonal transport and flagellar beating, are homologous at the fundamental level of the microtubule domains (the beta-tubulin peptide and we suggest a distinct but similarly located alpha-tubulin domain) mediating the attachment of tubulin-associated motors. |
| Keywords: | proteins; chromosome; brain; cilia; flagella; kinesin; movement; cytoplasmic dynein; invitro; dynein; alpha-tubulin; microtubule-based motility; sea-urchin sperm; squid axoplasm |
| Journal Title: | Cell Motility and the Cytoskeleton |
| Volume: | 20 |
| Issue: | 3 |
| ISSN: | 0886-1544 |
| Publisher: | Wiley Liss |
| Date Published: | 1991-01-01 |
| Start Page: | 249 |
| End Page: | 262 |
| Language: | English |
| ACCESSION: | WOS:A1991GR71400007 |
| DOI: | 10.1002/cm.970200308 |
| PROVIDER: | wos |
| PUBMED: | 1723030 |
| Notes: | Article -- Source: Wos |
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