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The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane

1998; Elsevier BV; Volume: 23; Issue: 8 Linguagem: Inglês

10.1016/s0968-0004(98)01237-7

1362-4326

Athar H. Chishti, Anthony C. Kim, Shirin M. Marfatia, Mohini Lutchman, Manjit Hanspal, Hitesh K. Jindal, Shih-Chun Liu, Philip S. Low, Guy A. Rouleau, Narla Mohandas, Joel Anne Chasis, John G. Conboy, Philippe Gascard, Yuichi Takakuwa, Shu‐Ching Huang, Edward J. Benz, Anthony Bretscher, Richard G. Fehon, James F. Gusella, Vijaya Ramesh, Frank Solomon, V. Marchesi, Shöichiro Tsukita, Sachiko Tsukita, Monique Arpin, Daniel Louvard, Nicholas K. Tonks, James M. Anderson, Alan S. Fanning, Peter J. Bryant, Daniel F. Woods, Kevin B. Hoover,

Vascular Malformations and Hemangiomas

Sequence analysis of the primary structures of members of a diverse group of proteins has revealed that they form a family of proteins that mediate linkage of the cytoskeleton to the plasma membrane (Fig. 1). A shared feature of these proteins is the presence of a domain that has been identified by several names: the amino-terminal domain; the 30-kDa domain; 4.1N30; the membrane–cytoskeletal-linking domain; the ERM-like domain; the ezrin-like domain of the band 4.1 superfamily; the conserved N-terminal region; and the membrane-attachment domain. To alleviate the confusion arising from a lack of any collective agreement, we propose to rename this domain FERM (F for 4.1 protein, E for ezrin, R for radixin and M for moesin), a name that reflects the initial identification of this domain in a family of peripheral membrane proteins that function as membrane–cytoskeleton linkers.