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Molecular roles of Myo1c function in lipid raft exocytosis

Lipid rafts are highly dynamic membrane subdomains enriched in specific protein and lipid components that create specialized ‘organizing’ platforms essential for an array of important cellular functions. The role of lipid rafts in membrane trafficking involves the constant remodelling of the plasma...

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Detalles Bibliográficos
Autores principales: Brandstaetter, Hemma, Kendrick-Jones, John, Buss, Folma
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3502219/
https://www.ncbi.nlm.nih.gov/pubmed/23739769
http://dx.doi.org/10.4161/cib.21201
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author Brandstaetter, Hemma
Kendrick-Jones, John
Buss, Folma
author_facet Brandstaetter, Hemma
Kendrick-Jones, John
Buss, Folma
author_sort Brandstaetter, Hemma
collection PubMed
description Lipid rafts are highly dynamic membrane subdomains enriched in specific protein and lipid components that create specialized ‘organizing’ platforms essential for an array of important cellular functions. The role of lipid rafts in membrane trafficking involves the constant remodelling of the plasma membrane through membrane uptake and balanced exocytosis of intracellular membranes. Our lab has identified the first motor protein, myosin 1c (Myo1c) involved in driving the recycling of lipid-raft enriched membranes from the perinuclear recycling compartment to the cell surface. This newly discovered role for Myo1c in lipid raft exocytosis is crucial for cell spreading, migration and pathogen entry; key cellular processes that require cell surface expansion and plasticity. Here we present a model suggesting Myo1c’s possible molecular functions in lipid raft recycling and discuss its wider implications for important cellular functions.
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spelling pubmed-35022192012-11-23 Molecular roles of Myo1c function in lipid raft exocytosis Brandstaetter, Hemma Kendrick-Jones, John Buss, Folma Commun Integr Biol Article Addendum Lipid rafts are highly dynamic membrane subdomains enriched in specific protein and lipid components that create specialized ‘organizing’ platforms essential for an array of important cellular functions. The role of lipid rafts in membrane trafficking involves the constant remodelling of the plasma membrane through membrane uptake and balanced exocytosis of intracellular membranes. Our lab has identified the first motor protein, myosin 1c (Myo1c) involved in driving the recycling of lipid-raft enriched membranes from the perinuclear recycling compartment to the cell surface. This newly discovered role for Myo1c in lipid raft exocytosis is crucial for cell spreading, migration and pathogen entry; key cellular processes that require cell surface expansion and plasticity. Here we present a model suggesting Myo1c’s possible molecular functions in lipid raft recycling and discuss its wider implications for important cellular functions. Landes Bioscience 2012-09-01 /pmc/articles/PMC3502219/ /pubmed/23739769 http://dx.doi.org/10.4161/cib.21201 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Article Addendum
Brandstaetter, Hemma
Kendrick-Jones, John
Buss, Folma
Molecular roles of Myo1c function in lipid raft exocytosis
title Molecular roles of Myo1c function in lipid raft exocytosis
title_full Molecular roles of Myo1c function in lipid raft exocytosis
title_fullStr Molecular roles of Myo1c function in lipid raft exocytosis
title_full_unstemmed Molecular roles of Myo1c function in lipid raft exocytosis
title_short Molecular roles of Myo1c function in lipid raft exocytosis
title_sort molecular roles of myo1c function in lipid raft exocytosis
topic Article Addendum
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3502219/
https://www.ncbi.nlm.nih.gov/pubmed/23739769
http://dx.doi.org/10.4161/cib.21201
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