The ins and outs of membrane bending by intrinsically disordered proteins

Author:

Yuan Feng1ORCID,Lee Christopher T.2ORCID,Sangani Arjun1ORCID,Houser Justin R.1,Wang Liping3,Lafer Eileen M.3ORCID,Rangamani Padmini2ORCID,Stachowiak Jeanne C.14ORCID

Affiliation:

1. Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA.

2. Department of Mechanical and Aerospace Engineering, University of California San Diego, La Jolla, CA, USA.

3. Department of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.

4. Department of Chemical Engineering, The University of Texas at Austin, Austin, TX, USA.

Abstract

Membrane curvature is essential to diverse cellular functions. While classically attributed to structured domains, recent work illustrates that intrinsically disordered proteins are also potent drivers of membrane bending. Specifically, repulsive interactions among disordered domains drive convex bending, while attractive interactions drive concave bending, creating membrane-bound, liquid-like condensates. How might disordered domains that contain both repulsive and attractive domains affect curvature? Here, we examined chimeras that combined attractive and repulsive interactions. When the attractive domain was closer to the membrane, its condensation amplified steric pressure among repulsive domains, leading to convex curvature. In contrast, when the repulsive domain was closer to the membrane, attractive interactions dominated, resulting in concave curvature. Further, a transition from convex to concave curvature occurred with increasing ionic strength, which reduced repulsion while enhancing condensation. In agreement with a simple mechanical model, these results illustrate a set of design rules for membrane bending by disordered proteins.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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