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

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

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

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.

Original languageEnglish
Article numbere04137
JournaleLife
Volume3
DOIs
StatePublished - Oct 10 2014

Keywords

  • E. coli
  • TALEN
  • adaptor
  • biochemistry
  • cell biology
  • clathrin
  • endocytosis
  • human

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