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Intrinsically disordered proteins drive membrane curvature

Author

Listed:
  • David J. Busch

    (The University of Texas at Austin)

  • Justin R. Houser

    (The University of Texas at Austin)

  • Carl C. Hayden

    (The University of Texas at Austin
    Sandia National Laboratories)

  • Michael B. Sherman

    (University of Texas Medical Branch)

  • Eileen M. Lafer

    (The University of Texas Health Science Center at San Antonio)

  • Jeanne C. Stachowiak

    (The University of Texas at Austin
    Institute for Cellular and Molecular Biology, The University of Texas at Austin)

Abstract

Assembly of highly curved membrane structures is essential to cellular physiology. The prevailing view has been that proteins with curvature-promoting structural motifs, such as wedge-like amphipathic helices and crescent-shaped BAR domains, are required for bending membranes. Here we report that intrinsically disordered domains of the endocytic adaptor proteins, Epsin1 and AP180 are highly potent drivers of membrane curvature. This result is unexpected since intrinsically disordered domains lack a well-defined three-dimensional structure. However, in vitro measurements of membrane curvature and protein diffusivity demonstrate that the large hydrodynamic radii of these domains generate steric pressure that drives membrane bending. When disordered adaptor domains are expressed as transmembrane cargo in mammalian cells, they are excluded from clathrin-coated pits. We propose that a balance of steric pressure on the two surfaces of the membrane drives this exclusion. These results provide quantitative evidence for the influence of steric pressure on the content and assembly of curved cellular membrane structures.

Suggested Citation

  • David J. Busch & Justin R. Houser & Carl C. Hayden & Michael B. Sherman & Eileen M. Lafer & Jeanne C. Stachowiak, 2015. "Intrinsically disordered proteins drive membrane curvature," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8875
    DOI: 10.1038/ncomms8875
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    Cited by:

    1. Daniel P. Arnold & Yaxin Xu & Sho C. Takatori, 2023. "Antibody binding reports spatial heterogeneities in cell membrane organization," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. San Hadži & Zala Živič & Matic Kovačič & Uroš Zavrtanik & Sarah Haesaerts & Daniel Charlier & Janez Plavec & Alexander N. Volkov & Jurij Lah & Remy Loris, 2024. "Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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