Cargando…

The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion

FMNL3 is a vertebrate-specific formin protein previously shown to play a role in angiogenesis and cell migration. Here we define the cellular localization of endogenous FMNL3, the dynamics of GFP-tagged FMNL3 during cell migration, and the effects of FMNL3 suppression in mammalian culture cells. The...

Descripción completa

Detalles Bibliográficos
Autores principales: Gauvin, Timothy J., Young, Lorna E., Higgs, Henry N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4310738/
https://www.ncbi.nlm.nih.gov/pubmed/25428984
http://dx.doi.org/10.1091/mbc.E14-07-1247
_version_ 1782354909009543168
author Gauvin, Timothy J.
Young, Lorna E.
Higgs, Henry N.
author_facet Gauvin, Timothy J.
Young, Lorna E.
Higgs, Henry N.
author_sort Gauvin, Timothy J.
collection PubMed
description FMNL3 is a vertebrate-specific formin protein previously shown to play a role in angiogenesis and cell migration. Here we define the cellular localization of endogenous FMNL3, the dynamics of GFP-tagged FMNL3 during cell migration, and the effects of FMNL3 suppression in mammalian culture cells. The majority of FMNL3 localizes in a punctate pattern, with >95% of these puncta being indistinguishable from the plasma membrane by fluorescence microscopy. A small number of dynamic cytoplasmic FMNL3 patches also exist, which enrich near cell–cell contact sites and fuse with the plasma membrane at these sites. These cytoplasmic puncta appear to be part of larger membranes of endocytic origin. On the plasma membrane, FMNL3 enriches particularly in filopodia and membrane ruffles and at nascent cell–cell adhesions. FMNL3-containing filopodia occur both at the cell–substratum interface and at cell–cell contacts, with the latter being 10-fold more stable. FMNL3 suppression by siRNA has two major effects: decrease in filopodia and compromised cell–cell adhesion in cells migrating as a sheet. Overall our results suggest that FMNL3 functions in assembly of actin-based protrusions that are specialized for cell–cell adhesion.
format Online
Article
Text
id pubmed-4310738
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-43107382015-04-16 The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion Gauvin, Timothy J. Young, Lorna E. Higgs, Henry N. Mol Biol Cell Articles FMNL3 is a vertebrate-specific formin protein previously shown to play a role in angiogenesis and cell migration. Here we define the cellular localization of endogenous FMNL3, the dynamics of GFP-tagged FMNL3 during cell migration, and the effects of FMNL3 suppression in mammalian culture cells. The majority of FMNL3 localizes in a punctate pattern, with >95% of these puncta being indistinguishable from the plasma membrane by fluorescence microscopy. A small number of dynamic cytoplasmic FMNL3 patches also exist, which enrich near cell–cell contact sites and fuse with the plasma membrane at these sites. These cytoplasmic puncta appear to be part of larger membranes of endocytic origin. On the plasma membrane, FMNL3 enriches particularly in filopodia and membrane ruffles and at nascent cell–cell adhesions. FMNL3-containing filopodia occur both at the cell–substratum interface and at cell–cell contacts, with the latter being 10-fold more stable. FMNL3 suppression by siRNA has two major effects: decrease in filopodia and compromised cell–cell adhesion in cells migrating as a sheet. Overall our results suggest that FMNL3 functions in assembly of actin-based protrusions that are specialized for cell–cell adhesion. The American Society for Cell Biology 2015-02-01 /pmc/articles/PMC4310738/ /pubmed/25428984 http://dx.doi.org/10.1091/mbc.E14-07-1247 Text en © 2015 Gauvin et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Gauvin, Timothy J.
Young, Lorna E.
Higgs, Henry N.
The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title_full The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title_fullStr The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title_full_unstemmed The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title_short The formin FMNL3 assembles plasma membrane protrusions that participate in cell–cell adhesion
title_sort formin fmnl3 assembles plasma membrane protrusions that participate in cell–cell adhesion
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4310738/
https://www.ncbi.nlm.nih.gov/pubmed/25428984
http://dx.doi.org/10.1091/mbc.E14-07-1247
work_keys_str_mv AT gauvintimothyj theforminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion
AT younglornae theforminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion
AT higgshenryn theforminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion
AT gauvintimothyj forminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion
AT younglornae forminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion
AT higgshenryn forminfmnl3assemblesplasmamembraneprotrusionsthatparticipateincellcelladhesion