Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis
During clathrin-mediated endocytosis in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for membrane invagination. Here authors present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membr...
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Nature Portfolio
2021
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oai:doaj.org-article:c76a9156443143ecaad0091e2cec9c082021-12-02T14:58:43ZStructure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis10.1038/s41467-021-23151-72041-1723https://doaj.org/article/c76a9156443143ecaad0091e2cec9c082021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23151-7https://doaj.org/toc/2041-1723During clathrin-mediated endocytosis in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for membrane invagination. Here authors present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membrane-binding domains from Sla2 and Ent1 bound to PIP2 that constitutes the anchor to the plasma membrane.Javier LizarrondoDavid P. KleblStephan NieblingMarc AbellaMartin A. SchroerHaydyn D. T. MertensKatharina VeithRoland ThuenauerDmitri I. SvergunMichal SkruznyFrank SobottStephen P. MuenchMaria M. Garcia-AlaiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-15 (2021) |
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Science Q Javier Lizarrondo David P. Klebl Stephan Niebling Marc Abella Martin A. Schroer Haydyn D. T. Mertens Katharina Veith Roland Thuenauer Dmitri I. Svergun Michal Skruzny Frank Sobott Stephen P. Muench Maria M. Garcia-Alai Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
description |
During clathrin-mediated endocytosis in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for membrane invagination. Here authors present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membrane-binding domains from Sla2 and Ent1 bound to PIP2 that constitutes the anchor to the plasma membrane. |
format |
article |
author |
Javier Lizarrondo David P. Klebl Stephan Niebling Marc Abella Martin A. Schroer Haydyn D. T. Mertens Katharina Veith Roland Thuenauer Dmitri I. Svergun Michal Skruzny Frank Sobott Stephen P. Muench Maria M. Garcia-Alai |
author_facet |
Javier Lizarrondo David P. Klebl Stephan Niebling Marc Abella Martin A. Schroer Haydyn D. T. Mertens Katharina Veith Roland Thuenauer Dmitri I. Svergun Michal Skruzny Frank Sobott Stephen P. Muench Maria M. Garcia-Alai |
author_sort |
Javier Lizarrondo |
title |
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
title_short |
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
title_full |
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
title_fullStr |
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
title_full_unstemmed |
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
title_sort |
structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/c76a9156443143ecaad0091e2cec9c08 |
work_keys_str_mv |
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