XMAP215 is a Processive Microtubule Polymerase

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XMAP215 is a Processive Microtubule Polymerase

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dc.contributor.author Hyman, Anthony A.
dc.contributor.author Howard, Jonathon
dc.contributor.author Harrison, Stephen
dc.contributor.author Kinoshita, Kazuhisa
dc.contributor.author Al-Bassam, Jawdat
dc.contributor.author Noetzel, Tim L.
dc.contributor.author Stear, Jeffrey H.
dc.contributor.author Brouhard, Gary J.
dc.date.accessioned 2009-06-30T20:44:30Z
dc.date.issued 2008
dc.identifier.citation Brouhard, Gary J., Jeffrey H. Stear, Tim L. Noetzel, Jawdat Al-Bassam, Kazuhisa Kinoshita, Stephen C. Harrison, Jonathon Howard, and Anthony A. Hyman. 2008. XMAP215 is a processive microtuble polymerase. Cell 132, no. 1: 79-88. en
dc.identifier.issn 0092-8674 en
dc.identifier.uri http://nrs.harvard.edu/urn-3:HUL.InstRepos:3128706
dc.description.abstract Fast growth of microtubules is essential for rapid assembly of the microtubule cytoskeleton during cell proliferation and differentiation. XMAP215 belongs to a conserved family of proteins that promote microtubule growth. To determine how XMAP215 accelerates growth, we developed a single-molecule assay to visualize directly XMAP215-GFP interacting with dynamic microtubules. XMAP215 binds free tubulin in a 1:1 complex that interacts with the microtubule lattice and targets the ends by a diffusion-facilitated mechanism. XMAP215 persists at the plus end for many rounds of tubulin subunit addition in a form of “tip-tracking.” These results show that XMAP215 is a processive polymerase that directly catalyzes the addition of up to 25 tubulin dimers to the growing plus end. Under some circumstances XMAP215 can also catalyze the reverse reaction, namely microtubule shrinkage. The similarities between XMAP215 and formins, actin polymerases, suggest that processive tip-tracking is a common mechanism for stimulating the growth of cytoskeletal polymers. en
dc.description.sponsorship Molecular and Cellular Biology en
dc.language.iso en_US en
dc.publisher Elsevier en
dc.relation.isversionof http://dx.doi.org/10.1016/j.cell.2007.11.043 en
dc.relation.hasversion http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=2311386&blobtype=pdf en
dash.license LAA
dc.title XMAP215 is a Processive Microtubule Polymerase en
dc.type Journal Article
dc.description.version Accepted Manuscript
dc.relation.journal Cell en
dash.depositing.author Harrison, Stephen

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  • FAS Scholarly Articles [6463]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University

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