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Regulation of a formin complex by the microtubule plus end protein tea1p

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dc.contributor.author Feierbach, Becket
dc.contributor.author Verde, Fulvia
dc.contributor.author Chang, Fred
dc.date.accessioned 2008-05-16T15:50:42Z
dc.date.available 2008-05-16T15:50:42Z
dc.date.issued 2004-06-07
dc.identifier.citation Journal of Cell Biology 165 (2004): 697-707 en
dc.identifier.uri http://hdl.handle.net/1912/2233
dc.description © 2004 Feierbach et al. This article is distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported License. The definitive version was published in Journal of Cell Biology 165 (2004): 697-707, doi:10.1083/jcb.200403090. en
dc.description.abstract The plus ends of microtubules have been speculated to regulate the actin cytoskeleton for the proper positioning of sites of cell polarization and cytokinesis. In the fission yeast Schizosaccharomyces pombe, interphase microtubules and the kelch repeat protein tea1p regulate polarized cell growth. Here, we show that tea1p is directly deposited at cell tips by microtubule plus ends. Tea1p associates in large "polarisome" complexes with bud6p and for3p, a formin that assembles actin cables. Tea1p also interacts in a separate complex with the CLIP-170 protein tip1p, a microtubule plus end–binding protein that anchors tea1p to the microtubule plus end. Localization experiments suggest that tea1p and bud6p regulate formin distribution and actin cable assembly. Although single mutants still polarize, for3{Delta}bud6{Delta}tea1{Delta} triple-mutant cells lack polarity, indicating that these proteins contribute overlapping functions in cell polarization. Thus, these experiments begin to elucidate how microtubules contribute to the proper spatial regulation of actin assembly and polarized cell growth. en
dc.description.sponsorship This research was supported by National Institutes of Health grant GM R01-GM56836, a research project grant from the American Cancer Society, a Nikon summer fellowship at the Marine Biological Laboratory (Woods Hole, MA) to F. Chang, and a National Institutes of Health postdoctoral fellowship (GM20283) to B. Feierbach. en
dc.format.mimetype application/pdf
dc.language.iso en_US en
dc.publisher Rockefeller University Press en
dc.relation.uri http://dx.doi.org/10.1083/jcb.200403090
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/ *
dc.subject Actin en
dc.subject Microtubules en
dc.subject Cell polarity en
dc.subject Fission yeast en
dc.subject formin en
dc.title Regulation of a formin complex by the microtubule plus end protein tea1p en
dc.type Article en
dc.identifier.doi 10.1083/jcb.200403090


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