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Cited by 1,044Cellular Mechanics and InteractionsProtein Kinase Regulation and GTPase SignalingCell Adhesion Molecules Research

Organizing the cell cortex: the role of ERM proteins

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Fehon, Richard G., McClatchey, Andrea I., Bretscher, Anthony·2010·Nature Reviews Molecular Cell Biology
DOI 10.1038/nrm2866PMC PMC2871950
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Abstract

Specialized membrane domains are an important feature of almost all cells. In particular, they are essential to tissues that have a highly organized cell cortex, such as the intestinal brush border epithelium. The ERM proteins (ezrin, radixin and moesin) have a crucial role in organizing membrane domains through their ability to interact with transmembrane proteins and the cytoskeleton. In doing so, they can provide structural links to strengthen the cell cortex and regulate the activities of signal transduction pathways. Recent studies examining the structure and in vivo functions of ERMs have greatly advanced our understanding of the importance of membrane-cytoskeleton interactions.

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  • The actin cytoskeleton provides rigidity to cells and is attached to the plasma membrane by ERM proteins.

    “The actin cytoskeleton provides rigidity to the cells and is attached to the plasma membrane by Ezrin, Radixin and Moesin, collectively known as ERM proteins [89,90].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [89]

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Authors
Fehon, R. G., McClatchey, A. I., & Bretscher, A.
Affiliations
  • University of Chicago (US)
  • Harvard University (US)
  • Cornell University (US)
ORCID
Venue
Nature Reviews Molecular Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2010-04
Volume
11
Issue
4
Pages
276-287
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
DOI
10.1038/nrm2866
PMC
PMC2871950
OpenAlex
W2042015318
Cited by
1,044
References
4
Citations by year
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FWCI
7.48
Type
journal article
Language
en
Update notices
erratum (2010-07-30)
Open access
Licence
Locations
  • Nature Reviews Molecular Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institute of General Medical Sciences (R01GM036652, R01GM087558)
  • National Institute of Neurological Disorders and Stroke (R01NS034783)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords
ezrin, moesin, radixin, ERM proteins, cell cortex, membrane domains, membrane-cytoskeleton interactions, transmembrane proteins, cytoskeleton, signal transduction, cell development, immune response
MeSH terms
Ezrin, Animals, Cytoskeletal Proteins, Cytoskeleton, Humans, Membrane Proteins, Microfilament Proteins, Microvilli, Signal Transduction

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