The ins and outs of membrane bending by intrinsically disordered proteins.

The ins and outs of membrane bending by intrinsically disordered proteins.
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DOI:
10.1126/sciadv.adg3485
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发表时间:
2023-07-07
期刊:
影响因子:
13.6
通讯作者:
Stachowiak, Jeanne C.
Stachowiak, Jeanne C.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Yuan, Feng;Lee, Christopher T.;Sangani, Arjun;Houser, Justin R.;Wang, Liping;Lafer, Eileen M.;Rangamani, Padmini;Stachowiak, Jeanne C.

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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. A set of design rules reveals how disordered proteins can impact membrane curvature.
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