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Published 7 June 2004. doi:10.1083/jcb.200403090
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 5, 697-707
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Article

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

Becket Feierbach1, Fulvia Verde2, and Fred Chang1,3

1 Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032
2 Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33136
3 Marine Biological Laboratory, Woods Hole, MA 02543

Address correspondence to Fred Chang, Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 W. 168th St., New York, NY 10032. Tel.: (212) 305-0252. Fax: (212) 305-1468. email: fc99{at}columbia.edu

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.

Key Words: actin; microtubules; cell polarity; fission yeast; formin

The online version of this article includes supplemental material.


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