ERM protein family

Ezrin/radixin/moesin family
Crystallographic structure of the N-terminal domain of moesin.[1]
Identifiers
SymbolERM
PfamPF00769
InterProIPR011259
SCOP21ef1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ef1​, 1e5w​, 1sgh​

The ERM protein family consists of three closely related proteins, ezrin,[2] radixin[3] and moesin.[4][5] The three paralogs, ezrin, radixin and moesin, are present in vertebrates, whereas other species have only one ERM gene. Therefore, in vertebrates these paralogs likely arose by gene duplication.[6]

ERM proteins are highly conserved throughout evolution. More than 75% identity is observed in the N-terminal and the C-terminal of vertebrates (ezrin, radixin, moesin), Drosophila (dmoesin) and C. elegans (ERM-1) homologs.[7]

  1. ^ PDB: 1E5W​; Edwards SD, Keep NH (June 2001). "The 2.7 Å crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation". Biochemistry. 40 (24): 7061–8. doi:10.1021/bi010419h. PMID 11401550.
  2. ^ Bretscher A (August 1983). "Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells". J. Cell Biol. 97 (2): 425–32. doi:10.1083/jcb.97.2.425. PMC 2112519. PMID 6885906.
  3. ^ Tsukita S, Hieda Y, Tsukita S (June 1989). "A new 82-kD barbed end-capping protein (radixin) localized in the cell- to-cell adherens junction: purification and characterization". J. Cell Biol. 108 (6): 2369–82. doi:10.1083/jcb.108.6.2369. PMC 2115614. PMID 2500445.
  4. ^ Lankes W, Griesmacher A, Grünwald J, Schwartz-Albiez R, Keller R (May 1988). "A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation". Biochem. J. 251 (3): 831–42. doi:10.1042/bj2510831. PMC 1149078. PMID 3046603.
  5. ^ Tsukita S, Yonemura S, Tsukita S (February 1997). "ERM proteins: head-to-tail regulation of actin-plasma membrane interaction". Trends Biochem. Sci. 22 (2): 53–8. doi:10.1016/S0968-0004(96)10071-2. PMID 9048483.
  6. ^ Bretscher A, Edwards K, Fehon RG (August 2002). "ERM proteins and merlin: integrators at the cell cortex". Nat Rev Mol Cell Biol. 3 (8): 586–99. doi:10.1038/nrm882. PMID 12154370. S2CID 26970178.
  7. ^ Fiévet B, Louvard D, Arpin M (May 2007). "ERM proteins in epithelial cell organization and functions". Biochim Biophys Acta. 1773 (5): 653–60. doi:10.1016/j.bbamcr.2006.06.013. PMID 16904765.