Definition
The ERM family consists of three closely related proteins, ezrin, radixin, and moesin. ERM proteins are cell membrane and cytoskeleton linker proteins.
Characteristics
History, Structure, and Sequence
Ezrin, the prototype ERM protein is a 585-amino acid polypeptide, first identified as a constituent of microvilli and shown to be present in actin-containing surface structure on a wide variety of cells. ERM proteins share homology in sequence structure and function. They are composed of three domains: an N-terminal globular domain; an extended α-helical domain; and a charged C-terminal domain. The N-terminal domain of ERM proteins is highly conserved and is also found in merlin, band 4.1 proteins, and members of the band 4.1 superfamily. This domain is called FERM (four.one protein, ezrin, radixin, moesin) domain. The crystal structure of moesin revealed that the FERM domain is composed of three structural modules that, together, form a compact...
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References
Bretscher A, Chambers D, Nguyen R et al (2000) ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu Rev Cell Dev Biol 16:113–143
Vaheri A, Carpen O, Heiska L et al (1997) The ezrin protein family: membrane-cytoskeleton interactions and disease associations. Curr Opin Cell Biol 9:659–666
Tsukita S, Yonemura S (1999) Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J Biol Chem 274:34507–34510
Bretscher A, Edwards K, Fehon RG (2002) ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 3:586–599
McClatchey AI (2003) Merlin and ERM proteins: unappreciated roles in cancer development? Nat Rev Cancer 3:877–883
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© 2011 Springer-Verlag Berlin Heidelberg
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Ren, L., Khanna, C. (2011). ERM Proteins. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16483-5_1990
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DOI: https://doi.org/10.1007/978-3-642-16483-5_1990
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