Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4.

Journal Article (Journal Article)

Mammalian septins constitute a family of at least 12 GTP-binding proteins that can form hetero-oligomers and that are sometimes found in association with actin or microtubule filaments. However, their functions are not understood. Using RNA interference, we found that suppression of septin expression in HeLa cells caused a pronounced increase in microtubule stability. Mass spectroscopic analysis of proteins coprecipitating with Sept6 identified the microtubule-associated protein MAP4 as a septin binding partner. A small, proline-rich region in the C-terminal half of MAP4 bound directly to a Sept 2:6:7 heterotrimer, and to the Sept2 monomer. The trimer blocked the ability of this MAP4 fragment to bind and bundle microtubules in vitro. In intact cells, MAP4 was required for the stabilization of microtubules induced by septin depletion. Moreover, septin depletion increased the number of cells with abnormal nuclei, and this effect was blocked by gene silencing of MAP4. These data identify a novel molecular function for septins in mammalian cells: the modulation of microtubule dynamics through interaction with MAP4.

Full Text

Duke Authors

Cited Authors

  • Kremer, BE; Haystead, T; Macara, IG

Published Date

  • October 2005

Published In

Volume / Issue

  • 16 / 10

Start / End Page

  • 4648 - 4659

PubMed ID

  • 16093351

Pubmed Central ID

  • PMC1237071

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.e05-03-0267


  • eng

Conference Location

  • United States