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• W2039444499 abstract "Microtubule (MT) crosslinking proteins of the ase1p/PRC1/Map65 family play a major role in the construction of MT networks such as the mitotic spindle. Most homologs in this family have been shown to localize with a remarkable specificity to sets of MTs that overlap with an antiparallel relative orientation [1Janson M.E. Loughlin R. Loïodice I. Fu C. Brunner D. Nédélec F.J. Tran P.T. Cross-linkers and motors organize dynamic microtubules to form stable bipolar arrays in fission yeast.Cell. 2007; 128: 357-368Abstract Full Text Full Text PDF PubMed Scopus (163) Google Scholar, 2Loiodice I. Staub J. Setty T.G. Nguyen N.P.T. Paoletti A. Tran P.T. Ase1p organizes antiparallel microtubule arrays during interphase and mitosis in fission yeast.Mol. Biol. Cell. 2005; 16: 1756-1768Crossref PubMed Scopus (138) Google Scholar, 3Schuyler S.C. Liu J.Y. Pellman D. The molecular function of Ase1p: Evidence for a MAP-dependent midzone-specific spindle matrix.J. Cell Biol. 2003; 160: 517-528Crossref PubMed Scopus (162) Google Scholar, 4Yamashita A. Sato M. Fujita A. Yamamoto M. Toda T. The roles of fission yeast Ase1 in mitotic cell division, meiotic nuclear oscillation, and cytokinesis checkpoint signaling.Mol. Biol. Cell. 2005; 16: 1378-1395Crossref PubMed Scopus (114) Google Scholar]. Regulatory proteins bind to ase1p/PRC1/Map65 and appear to use the localization to set up precise spatial signals [5Ban R. Irino Y. Fukami K. Tanaka H. Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase.J. Biol. Chem. 2004; 279: 16394-16402Crossref PubMed Scopus (66) Google Scholar, 6Bratman S.V. Chang F. Stabilization of overlapping microtubules by fission yeast CLASP.Dev. Cell. 2007; 13: 812-827Abstract Full Text Full Text PDF PubMed Scopus (86) Google Scholar, 7Gruneberg U. Neef R. Li X.L. Chan E.H.Y. Chalamalasetty R.B. Nigg E.A. Barr F.A. KIF14 and citron kinase act together to promote efficient cytokinesis.J. Cell Biol. 2006; 172: 363-372Crossref PubMed Scopus (197) Google Scholar, 8Kurasawa Y. Earnshaw W.C. Mochizuki Y. Dohmae N. Todokoro K. Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation.EMBO J. 2004; 23: 3237-3248Crossref PubMed Scopus (232) Google Scholar, 9Neef R. Gruneberg U. Kopajtich R. Li X.L. Nigg E.A. Sillje H. Barr F.A. Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1.Nat. Cell Biol. 2007; 9: 436-444Crossref PubMed Scopus (192) Google Scholar, 10Zhu C.J. Jiang W. Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is essential for midzone formation and cytokinesis.Proc. Natl. Acad. Sci. USA. 2005; 102: 343-348Crossref PubMed Scopus (220) Google Scholar]. Here, we present evidence for a mechanism of localized protein multimerization underlying the specific targeting of ase1p, the fision yeast homolog. In controlled in vitro experiments, dimers of ase1-GFP diffused along the surface of single MTs and, at concentrations above a certain threshold, assembled into static multimeric structures. We observed that this threshold was significantly lower on overlapping MTs. We also observed diffusion and multimerization of ase1-GFP on MTs inside living cells, suggesting that a multimerization-driven localization mechanism is relevant in vivo. The domains responsible for MT binding and multimerization were identified via a series of ase1p truncations. Our findings show that cells use a finely tuned cooperative localization mechanism that exploits differences in the geometry and concentration of ase1p binding sites along single and overlapping MTs." @default.
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• W2039444499 date "2008-11-01" @default.
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• W2039444499 title "Microtubule-Driven Multimerization Recruits ase1p onto Overlapping Microtubules" @default.
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• W2039444499 doi "https://doi.org/10.1016/j.cub.2008.09.046" @default.
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