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

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

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...

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Main Authors: Umasankar, Perunthottathu K, Ma, Li, Thieman, James R, Jha, Anupma, Doray, Balraj, Watkins, Simon C, Traub, Linton M
Format: Online
Language:English
Published: eLife Sciences Publications, Ltd 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4215538/
id pubmed-4215538
recordtype oai_dc
spelling pubmed-42155382014-11-21 A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing Umasankar, Perunthottathu K Ma, Li Thieman, James R Jha, Anupma Doray, Balraj Watkins, Simon C Traub, Linton M Biochemistry 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. eLife Sciences Publications, Ltd 2014-10-10 /pmc/articles/PMC4215538/ /pubmed/25303365 http://dx.doi.org/10.7554/eLife.04137 Text en Copyright © 2014, Umasankar et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Umasankar, Perunthottathu K
Ma, Li
Thieman, James R
Jha, Anupma
Doray, Balraj
Watkins, Simon C
Traub, Linton M
spellingShingle Umasankar, Perunthottathu K
Ma, Li
Thieman, James R
Jha, Anupma
Doray, Balraj
Watkins, Simon C
Traub, Linton M
A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
author_facet Umasankar, Perunthottathu K
Ma, Li
Thieman, James R
Jha, Anupma
Doray, Balraj
Watkins, Simon C
Traub, Linton M
author_sort Umasankar, Perunthottathu K
title A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
title_short A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
title_full A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
title_fullStr A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
title_full_unstemmed A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
title_sort clathrin coat assembly role for the muniscin protein central linker revealed by talen-mediated gene editing
description 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.
publisher eLife Sciences Publications, Ltd
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4215538/
_version_ 1613150834842927104

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