Cargando…
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...
Autores principales: | , , , , , |
---|---|
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 |
_version_ | 1783256333088194560 |
---|---|
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. |
format | Online Article Text |
id | pubmed-5551697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT farrellkristenb novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis AT mcdonaldseth novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis AT lambandrewk novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis AT worcestercolette novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis AT peersenolveb novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis AT dipietrosantiagom novelfunctionofadyneinlightchaininactinassemblyduringclathrinmediatedendocytosis |