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Membranes are more mosaic than fluid

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  • Donald M. Engelman

    (Yale University)

Abstract

The wealth of new data on membrane protein structures and functions is changing our general view of membrane architecture. Some of the key themes that are emerging are that membranes are patchy, with segregated regions of structure and function, that lipid regions vary in thickness and composition, and that crowding and ectodomains limit exposure of lipid to the adjacent aqueous regions.

Suggested Citation

  • Donald M. Engelman, 2005. "Membranes are more mosaic than fluid," Nature, Nature, vol. 438(7068), pages 578-580, December.
    • Handle: RePEc:nat:nature:v:438:y:2005:i:7068:d:10.1038_nature04394
    DOI: 10.1038/nature04394
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    Cited by:

    1. Alexandre Pozza & François Giraud & Quentin Cece & Marina Casiraghi & Elodie Point & Marjorie Damian & Christel Le Bon & Karine Moncoq & Jean-Louis Banères & Ewen Lescop & Laurent J. Catoire, 2022. "Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Shi, Yu & Eze, Chika & Xiong, Binyu & He, Weidong & Zhang, Han & Lim, T.M. & Ukil, A. & Zhao, Jiyun, 2019. "Recent development of membrane for vanadium redox flow battery applications: A review," Applied Energy, Elsevier, vol. 238(C), pages 202-224.
    3. Stefania A. Mari & Kristyna Pluhackova & Joka Pipercevic & Matthew Leipner & Sebastian Hiller & Andreas Engel & Daniel J. Müller, 2022. "Gasdermin-A3 pore formation propagates along variable pathways," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Yining Jiang & Batiste Thienpont & Vinay Sapuru & Richard K. Hite & Jeremy S. Dittman & James N. Sturgis & Simon Scheuring, 2022. "Membrane-mediated protein interactions drive membrane protein organization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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