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Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis

Clathrin- and actin-mediated endocytosis is essential in eukaryotic cells. In this study, we demonstrate that Tda2 is a novel protein of the endocytic machinery necessary for normal internalization of native cargo in yeast. Tda2 has not been classified in any protein family. Unexpectedly, solving th...

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Detalles Bibliográficos
Autores principales: Farrell, Kristen B., McDonald, Seth, Lamb, Andrew K., Worcester, Colette, Peersen, Olve B., Di Pietro, Santiago M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5551697/
https://www.ncbi.nlm.nih.gov/pubmed/28706108
http://dx.doi.org/10.1083/jcb.201604123
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author Farrell, Kristen B.
McDonald, Seth
Lamb, Andrew K.
Worcester, Colette
Peersen, Olve B.
Di Pietro, Santiago M.
author_facet Farrell, Kristen B.
McDonald, Seth
Lamb, Andrew K.
Worcester, Colette
Peersen, Olve B.
Di Pietro, Santiago M.
author_sort Farrell, Kristen B.
collection PubMed
description Clathrin- and actin-mediated endocytosis is essential in eukaryotic cells. In this study, we demonstrate that Tda2 is a novel protein of the endocytic machinery necessary for normal internalization of native cargo in yeast. Tda2 has not been classified in any protein family. Unexpectedly, solving the crystal structure of Tda2 revealed it belongs to the dynein light chain family. However, Tda2 works independently of the dynein motor complex and microtubules. Tda2 forms a tight complex with the polyproline motif–rich protein Aim21, which interacts physically with the SH3 domain of the Arp2/3 complex regulator Bbc1. The Tda2–Aim21 complex localizes to endocytic sites in a Bbc1- and filamentous actin–dependent manner. Importantly, the Tda2–Aim21 complex interacts directly with and facilitates the recruitment of actin-capping protein, revealing barbed-end filament capping at endocytic sites to be a regulated event. Thus, we have uncovered a new layer of regulation of the actin cytoskeleton by a member of a conserved protein family that has not been previously associated with a function in endocytosis.
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spelling pubmed-55516972018-02-07 Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis Farrell, Kristen B. McDonald, Seth Lamb, Andrew K. Worcester, Colette Peersen, Olve B. Di Pietro, Santiago M. J Cell Biol Research Articles Clathrin- and actin-mediated endocytosis is essential in eukaryotic cells. In this study, we demonstrate that Tda2 is a novel protein of the endocytic machinery necessary for normal internalization of native cargo in yeast. Tda2 has not been classified in any protein family. Unexpectedly, solving the crystal structure of Tda2 revealed it belongs to the dynein light chain family. However, Tda2 works independently of the dynein motor complex and microtubules. Tda2 forms a tight complex with the polyproline motif–rich protein Aim21, which interacts physically with the SH3 domain of the Arp2/3 complex regulator Bbc1. The Tda2–Aim21 complex localizes to endocytic sites in a Bbc1- and filamentous actin–dependent manner. Importantly, the Tda2–Aim21 complex interacts directly with and facilitates the recruitment of actin-capping protein, revealing barbed-end filament capping at endocytic sites to be a regulated event. Thus, we have uncovered a new layer of regulation of the actin cytoskeleton by a member of a conserved protein family that has not been previously associated with a function in endocytosis. The Rockefeller University Press 2017-08-07 /pmc/articles/PMC5551697/ /pubmed/28706108 http://dx.doi.org/10.1083/jcb.201604123 Text en © 2017 Farrell et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Farrell, Kristen B.
McDonald, Seth
Lamb, Andrew K.
Worcester, Colette
Peersen, Olve B.
Di Pietro, Santiago M.
Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title_full Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title_fullStr Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title_full_unstemmed Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title_short Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
title_sort novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5551697/
https://www.ncbi.nlm.nih.gov/pubmed/28706108
http://dx.doi.org/10.1083/jcb.201604123
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