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Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing

Author

Listed:
  • Wade F. Zeno

    (The University of Texas at Austin)

  • Upayan Baul

    (The University of Texas at Austin)

  • Wilton T. Snead

    (The University of Texas at Austin)

  • Andre C. M. DeGroot

    (The University of Texas at Austin)

  • Liping Wang

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

  • Eileen M. Lafer

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

  • D. Thirumalai

    (The University of Texas at Austin)

  • Jeanne C. Stachowiak

    (The University of Texas at Austin
    The University of Texas at Austin)

Abstract

The ability of proteins to sense membrane curvature is essential to cellular function. All known sensing mechanisms rely on protein domains with specific structural features such as wedge-like amphipathic helices and crescent-shaped BAR domains. Yet many proteins that contain these domains also contain large intrinsically disordered regions. Here we report that disordered domains are themselves potent sensors of membrane curvature. Comparison of Monte Carlo simulations with in vitro and live-cell measurements demonstrates that the polymer-like behavior of disordered domains found in endocytic proteins drives them to partition preferentially to convex membrane surfaces, which place fewer geometric constraints on their conformational entropy. Further, proteins containing both structured curvature sensors and disordered regions are more than twice as curvature sensitive as their respective structured domains alone. These findings demonstrate an entropic mechanism of curvature sensing that is independent of protein structure and illustrate how structured and disordered domains can synergistically enhance curvature sensitivity.

Suggested Citation

  • Wade F. Zeno & Upayan Baul & Wilton T. Snead & Andre C. M. DeGroot & Liping Wang & Eileen M. Lafer & D. Thirumalai & Jeanne C. Stachowiak, 2018. "Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06532-3
    DOI: 10.1038/s41467-018-06532-3
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    Cited by:

    1. F. Emil Thomasen & Tórur Skaalum & Ashutosh Kumar & Sriraksha Srinivasan & Stefano Vanni & Kresten Lindorff-Larsen, 2024. "Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Chih-Hao Lu & Kayvon Pedram & Ching-Ting Tsai & Taylor Jones & Xiao Li & Melissa L. Nakamoto & Carolyn R. Bertozzi & Bianxiao Cui, 2022. "Membrane curvature regulates the spatial distribution of bulky glycoproteins," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Yiming Yu & Shige H. Yoshimura, 2023. "Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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