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

Publication ,  Journal Article
Kremer, BE; Haystead, T; Macara, IG
Published in: Mol Biol Cell
October 2005

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.

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Published In

Mol Biol Cell

DOI

ISSN

1059-1524

Publication Date

October 2005

Volume

16

Issue

10

Start / End Page

4648 / 4659

Location

United States

Related Subject Headings

  • Septins
  • RNA, Small Interfering
  • Protein Binding
  • Phosphoric Monoester Hydrolases
  • Molecular Sequence Data
  • Mitosis
  • Microtubules
  • Microtubule-Associated Proteins
  • Humans
  • Hela Cells
 

Citation

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Kremer, B. E., Haystead, T., & Macara, I. G. (2005). Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell, 16(10), 4648–4659. https://doi.org/10.1091/mbc.e05-03-0267
Kremer, Brandon E., Timothy Haystead, and Ian G. Macara. “Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4.Mol Biol Cell 16, no. 10 (October 2005): 4648–59. https://doi.org/10.1091/mbc.e05-03-0267.
Kremer BE, Haystead T, Macara IG. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell. 2005 Oct;16(10):4648–59.
Kremer, Brandon E., et al. “Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4.Mol Biol Cell, vol. 16, no. 10, Oct. 2005, pp. 4648–59. Pubmed, doi:10.1091/mbc.e05-03-0267.
Kremer BE, Haystead T, Macara IG. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell. 2005 Oct;16(10):4648–4659.

Published In

Mol Biol Cell

DOI

ISSN

1059-1524

Publication Date

October 2005

Volume

16

Issue

10

Start / End Page

4648 / 4659

Location

United States

Related Subject Headings

  • Septins
  • RNA, Small Interfering
  • Protein Binding
  • Phosphoric Monoester Hydrolases
  • Molecular Sequence Data
  • Mitosis
  • Microtubules
  • Microtubule-Associated Proteins
  • Humans
  • Hela Cells