Protein Domain : Ezrin/radixin/moesin, alpha-helical domain IPR046810

Type	Domain
Description	The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [ , ]. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin-binding protein []. ERM proteins crosslink actin filaments with plasma membranes. They co-localise with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains []. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein) []. ERM molecules contain 3 domains, an N-terminal globular domain, an extended α-helical domain and a charged C-terminal domain () [ ]. Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. This entry represents the α-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, that regulate the activity of these proteins [, ].
Short Name	ERM_helical