Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Zhu, H.
  • Coppinger, J. A.
  • Jang, C. Y.
  • Yates III, John
  • Fang, G. W.

publication date

  • 2008

journal

  • Journal of Cell Biology  Journal

abstract

  • Microtubules (MTs) are nucleated from centrosomes and chromatin. In addition, MTs can be generated from preexiting MTs in a gamma-tubulin-dependent manner in yeast, plant, and Drosophila cells, although the underlying mechanism remains unknown. Here we show the spindle-associated protein FAM29A promotes MT-dependent MT amplification and is required for efficient chromosome congression and segregation in mammalian cells. Depletion of FAM29A reduces spindle MT density. FAM29A is not involved in the nucleation of MTs from centrosomes and chromatin, but is required for a subsequent increase in MT mass in cells released from nocodazole. FAM29A interacts with the NEDD1-gamma-tubulin complex and recruits this complex to the spindle, which, in turn, promotes MT polymerization. FAM29A preferentially associates with kinetochore MTs and knockdown of FAM29A reduces the number of MTs in a kinetochore fiber, activates the spindle checkpoint, and delays the mitotic progression. Our study provides a biochemical mechanism for MT-dependent MT amplification and for the maturation of kinetochore fibers in mammalian cells.

subject areas

  • Centrosome
  • Chromatin
  • HeLa Cells
  • Humans
  • Kinetochores
  • Microtubule-Associated Proteins
  • Microtubules
  • Mitosis
  • Spindle Apparatus
  • Time Factors
  • Tubulin
scroll to property group menus

Identity

PubMed Central ID

  • PMC2592839

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200807046

PubMed ID

  • 19029337
scroll to property group menus

Additional Document Info

start page

  • 835

end page

  • 848

volume

  • 183

issue

  • 5

©2019 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support