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通过TALEN介导的基因编辑揭示了muniscin蛋白中心连接体在网格蛋白包被组装中的作用。

A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing.

作者信息

Umasankar Perunthottathu K, Ma Li, Thieman James R, Jha Anupma, Doray Balraj, Watkins Simon C, Traub Linton M

机构信息

Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, United States.

Department of Medicine, Washington University School of Medicine, St. Louis, United States.

出版信息

Elife. 2014 Oct 10;3:e04137. doi: 10.7554/eLife.04137.

DOI:10.7554/eLife.04137
PMID:25303365
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4215538/
Abstract

Clathrin-mediated endocytosis is an evolutionarily ancient membrane transport system regulating cellular receptivity and responsiveness. Plasmalemma clathrin-coated structures range from unitary domed assemblies to expansive planar constructions with internal or flanking invaginated buds. Precisely how these morphologically-distinct coats are formed, and whether all are functionally equivalent for selective cargo internalization is still disputed. We have disrupted the genes encoding a set of early arriving clathrin-coat constituents, FCHO1 and FCHO2, in HeLa cells. Endocytic coats do not disappear in this genetic background; rather clustered planar lattices predominate and endocytosis slows, but does not cease. The central linker of FCHO proteins acts as an allosteric regulator of the prime endocytic adaptor, AP-2. By loading AP-2 onto the plasma membrane, FCHO proteins provide a parallel pathway for AP-2 activation and clathrin-coat fabrication. Further, the steady-state morphology of clathrin-coated structures appears to be a manifestation of the availability of the muniscin linker during lattice polymerization.

摘要

网格蛋白介导的内吞作用是一种进化上古老的膜转运系统，可调节细胞的感受性和反应性。质膜上的网格蛋白包被结构范围从单一的穹顶状组装体到具有内部或侧翼内陷芽的扩展平面结构。这些形态上不同的包被究竟是如何形成的，以及它们在选择性货物内化方面是否都具有功能等效性，仍然存在争议。我们已经在HeLa细胞中破坏了编码一组早期到达的网格蛋白包被成分FCHO1和FCHO2的基因。在这种遗传背景下，内吞包被不会消失；相反，聚集的平面晶格占主导，内吞作用减慢，但不会停止。FCHO蛋白的中央连接子作为主要内吞衔接蛋白AP-2的变构调节剂。通过将AP-2加载到质膜上，FCHO蛋白为AP-2激活和网格蛋白包被的形成提供了一条平行途径。此外，网格蛋白包被结构的稳态形态似乎是网格蛋白聚合过程中muniscin连接子可用性的一种表现。

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