Cargando…

Clathrin-containing adhesion complexes

An understanding of the mechanisms whereby cell adhesion complexes (ACs) relay signals bidirectionally across the plasma membrane is necessary to interpret the role of adhesion in regulating migration, differentiation, and growth. A range of AC types has been defined, but to date all have similar co...

Descripción completa

Detalles Bibliográficos
Autores principales: Lock, John G., Baschieri, Francesco, Jones, Matthew C., Humphries, Jonathan D., Montagnac, Guillaume, Strömblad, Staffan, Humphries, Martin J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6605790/
https://www.ncbi.nlm.nih.gov/pubmed/31208994
http://dx.doi.org/10.1083/jcb.201811160
_version_ 1783431829786722304
author Lock, John G.
Baschieri, Francesco
Jones, Matthew C.
Humphries, Jonathan D.
Montagnac, Guillaume
Strömblad, Staffan
Humphries, Martin J.
author_facet Lock, John G.
Baschieri, Francesco
Jones, Matthew C.
Humphries, Jonathan D.
Montagnac, Guillaume
Strömblad, Staffan
Humphries, Martin J.
author_sort Lock, John G.
collection PubMed
description An understanding of the mechanisms whereby cell adhesion complexes (ACs) relay signals bidirectionally across the plasma membrane is necessary to interpret the role of adhesion in regulating migration, differentiation, and growth. A range of AC types has been defined, but to date all have similar compositions and are dependent on a connection to the actin cytoskeleton. Recently, a new class of AC has been reported that normally lacks association with both the cytoskeleton and integrin-associated adhesome components, but is rich in components of the clathrin-mediated endocytosis machinery. The characterization of this new type of adhesion structure, which is emphasized by mitotic cells and cells in long-term culture, identifies a hitherto underappreciated link between the adhesion machinery and clathrin structures at the plasma membrane. While this discovery has implications for how ACs are assembled and disassembled, it raises many other issues. Consequently, to increase awareness within the field, and stimulate research, we explore a number of the most significant questions below.
format Online
Article
Text
id pubmed-6605790
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-66057902020-01-01 Clathrin-containing adhesion complexes Lock, John G. Baschieri, Francesco Jones, Matthew C. Humphries, Jonathan D. Montagnac, Guillaume Strömblad, Staffan Humphries, Martin J. J Cell Biol Reviews An understanding of the mechanisms whereby cell adhesion complexes (ACs) relay signals bidirectionally across the plasma membrane is necessary to interpret the role of adhesion in regulating migration, differentiation, and growth. A range of AC types has been defined, but to date all have similar compositions and are dependent on a connection to the actin cytoskeleton. Recently, a new class of AC has been reported that normally lacks association with both the cytoskeleton and integrin-associated adhesome components, but is rich in components of the clathrin-mediated endocytosis machinery. The characterization of this new type of adhesion structure, which is emphasized by mitotic cells and cells in long-term culture, identifies a hitherto underappreciated link between the adhesion machinery and clathrin structures at the plasma membrane. While this discovery has implications for how ACs are assembled and disassembled, it raises many other issues. Consequently, to increase awareness within the field, and stimulate research, we explore a number of the most significant questions below. Rockefeller University Press 2019-07-01 2019-06-17 /pmc/articles/PMC6605790/ /pubmed/31208994 http://dx.doi.org/10.1083/jcb.201811160 Text en © 2019 Lock 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 Reviews
Lock, John G.
Baschieri, Francesco
Jones, Matthew C.
Humphries, Jonathan D.
Montagnac, Guillaume
Strömblad, Staffan
Humphries, Martin J.
Clathrin-containing adhesion complexes
title Clathrin-containing adhesion complexes
title_full Clathrin-containing adhesion complexes
title_fullStr Clathrin-containing adhesion complexes
title_full_unstemmed Clathrin-containing adhesion complexes
title_short Clathrin-containing adhesion complexes
title_sort clathrin-containing adhesion complexes
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6605790/
https://www.ncbi.nlm.nih.gov/pubmed/31208994
http://dx.doi.org/10.1083/jcb.201811160
work_keys_str_mv AT lockjohng clathrincontainingadhesioncomplexes
AT baschierifrancesco clathrincontainingadhesioncomplexes
AT jonesmatthewc clathrincontainingadhesioncomplexes
AT humphriesjonathand clathrincontainingadhesioncomplexes
AT montagnacguillaume clathrincontainingadhesioncomplexes
AT strombladstaffan clathrincontainingadhesioncomplexes
AT humphriesmartinj clathrincontainingadhesioncomplexes