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A class of dynamin-like GTPases involved in the generation of the tubular ER network.

The endoplasmic reticulum (ER) consists of tubules that are shaped by the reticulons and DP1/Yop1p, but how the tubules form an interconnected network is unknown. Here, we show that mammalian atlastins, which are dynamin-like, integral membrane GTPases, interact with the tubule-shaping proteins. The atlastins localize to the tubular ER and are required for proper network formation in vivo and in vitro. Depletion of the atlastins or overexpression of dominant-negative forms inhibits tubule interconnections. The Sey1p GTPase in S. cerevisiae is likely a functional ortholog of the atlastins; it shares the same signature motifs and membrane topology and interacts genetically and physically with the tubule-shaping proteins. Cells simultaneously lacking Sey1p and a tubule-shaping protein have ER morphology defects. These results indicate that formation of the tubular ER network depends on conserved dynamin-like GTPases. Since atlastin-1 mutations cause a common form of hereditary spastic paraplegia, we suggest ER-shaping defects as a neuropathogenic mechanism.

Pubmed ID: 19665976

Authors

  • Hu J
  • Shibata Y
  • Zhu PP
  • Voss C
  • Rismanchi N
  • Prinz WA
  • Rapoport TA
  • Blackstone C

Journal

Cell

Publication Data

August 7, 2009

Associated Grants

  • Agency: Howard Hughes Medical Institute, Id:
  • Agency: Howard Hughes Medical Institute, Id:
  • Agency: Intramural NIH HHS, Id:

Mesh Terms

  • Animals
  • Dynamin I
  • Dynamins
  • Endoplasmic Reticulum
  • GTP Phosphohydrolases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins