ERM proteins and merlin: integrators at the cell cortex
Abstract
A fundamental property of many plasma-membrane proteins is their association with the underlying cytoskeleton to determine cell shape, and to participate in adhesion, motility and other plasma-membrane processes, including endocytosis and exocytosis. The ezrin-radixin-moesin (ERM) proteins are crucial components that provide a regulated linkage between membrane proteins and the cortical cytoskeleton, and also participate in signal-transduction pathways. The closely related tumour suppressor merlin shares many properties with ERM proteins, yet also provides a distinct and essential function.
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The FERM domain forms the signature for members of the ERM family of proteins and is known to mediate the interaction between membranes and membrane proteins.
“The FERM domain forms the signature for members of the ERM family of proteins and is known to mediate the interaction between membranes and membrane proteins (21).”
IDOL is a unique ERM family member in that it contains a RING unit in addition to the signature FERM domain.
“IDOL is a unique ERM family member in that it contains a RING unit in addition to the signature FERM domain (10,21).”
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- Authors
- Bretscher, A., Edwards, K., & Fehon, R. G.
- Affiliations
- Cornell University (US)
- Illinois State University (US)
- Duke University (US)
- Corresponding author
- Bretscher, Anthony
- Edwards, Kevin
- Fehon, Richard G.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2002-08
- Volume
- 3
- Issue
- 8
- Pages
- 586-599
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2005252392
- Cited by
- 1,306
- References
- 0
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 23 · 2023: 29 · 2022: 33 · 2021: 43 · 2020: 31 · 2019: 31 · 2018: 32 · 2017: 44 · 2016: 40 · 2015: 56 · 2014: 73 · 2013: 61 · 2012: 69
- FWCI
- 5.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- 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-radixin-moesin proteins, Merlin, cell cortex, cell shape, cell adhesion, cell motility, endocytosis, exocytosis, signal transduction, tumour suppressor
- MeSH terms
- Ezrin, Animals, Blood Proteins, Cell Line, Cell Membrane, Cytoskeletal Proteins, Cytoskeleton, Multigene Family, Humans, Membrane Proteins, Microfilament Proteins, Models, Biological, Phosphoproteins, Phylogeny, Signal Transduction, Cell Polarity, Protein Structure, Tertiary, Tumor Suppressor Proteins, Neurofibromin 2
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