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Generation of high curvature membranes mediated by direct endophilin bilayer interactions.

Publication ,  Journal Article
Farsad, K; Ringstad, N; Takei, K; Floyd, SR; Rose, K; De Camilli, P
Published in: J Cell Biol
October 15, 2001

Endophilin 1 is a presynaptically enriched protein which binds the GTPase dynamin and the polyphosphoinositide phosphatase synptojanin. Perturbation of endophilin function in cell-free systems and in a living synapse has implicated endophilin in endocytic vesicle budding (Ringstad, N., H. Gad, P. Low, G. Di Paolo, L. Brodin, O. Shupliakov, and P. De Camilli. 1999. Neuron. 24:143-154; Schmidt, A., M. Wolde, C. Thiele, W. Fest, H. Kratzin, A.V. Podtelejnikov, W. Witke, W.B. Huttner, and H.D. Soling. 1999. Nature. 401:133-141; Gad, H., N. Ringstad, P. Low, O. Kjaerulff, J. Gustafsson, M. Wenk, G. Di Paolo, Y. Nemoto, J. Crun, M.H. Ellisman, et al. 2000. Neuron. 27:301-312). Here, we show that purified endophilin can directly bind and evaginate lipid bilayers into narrow tubules similar in diameter to the neck of a clathrin-coated bud, providing new insight into the mechanisms through which endophilin may participate in membrane deformation and vesicle budding. This property of endophilin is independent of its putative lysophosphatydic acid acyl transferase activity, is mediated by its NH2-terminal region, and requires an amino acid stretch homologous to a corresponding region in amphiphysin, a protein previously shown to have similar effects on lipid bilayers (Takei, K., V.I. Slepnev, V. Haucke, and P. De Camilli. 1999. Nat. Cell Biol. 1:33-39). Endophilin cooligomerizes with dynamin rings on lipid tubules and inhibits dynamin's GTP-dependent vesiculating activity. Endophilin B, a protein with homology to endophilin 1, partially localizes to the Golgi complex and also deforms lipid bilayers into tubules, underscoring a potential role of endophilin family members in diverse tubulovesicular membrane-trafficking events in the cell.

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Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

October 15, 2001

Volume

155

Issue

2

Start / End Page

193 / 200

Location

United States

Related Subject Headings

  • Synaptic Vesicles
  • Sequence Homology, Amino Acid
  • Rats
  • Protein Structure, Tertiary
  • Phylogeny
  • Nerve Tissue Proteins
  • Molecular Sequence Data
  • Macromolecular Substances
  • Lipid Bilayers
  • Humans
 

Citation

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Farsad, K., Ringstad, N., Takei, K., Floyd, S. R., Rose, K., & De Camilli, P. (2001). Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol, 155(2), 193–200. https://doi.org/10.1083/jcb.200107075
Farsad, K., N. Ringstad, K. Takei, S. R. Floyd, K. Rose, and P. De Camilli. “Generation of high curvature membranes mediated by direct endophilin bilayer interactions.J Cell Biol 155, no. 2 (October 15, 2001): 193–200. https://doi.org/10.1083/jcb.200107075.
Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol. 2001 Oct 15;155(2):193–200.
Farsad, K., et al. “Generation of high curvature membranes mediated by direct endophilin bilayer interactions.J Cell Biol, vol. 155, no. 2, Oct. 2001, pp. 193–200. Pubmed, doi:10.1083/jcb.200107075.
Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol. 2001 Oct 15;155(2):193–200.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

October 15, 2001

Volume

155

Issue

2

Start / End Page

193 / 200

Location

United States

Related Subject Headings

  • Synaptic Vesicles
  • Sequence Homology, Amino Acid
  • Rats
  • Protein Structure, Tertiary
  • Phylogeny
  • Nerve Tissue Proteins
  • Molecular Sequence Data
  • Macromolecular Substances
  • Lipid Bilayers
  • Humans