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FERM domain

The current understanding on activation of Tec kinases fits into a two-step model. In the first step an intramolecular interaction between the SH3 domain and aproline-rich region in the TH domain is disrupted by binding ofthe PH domain to phosphoinositides, G protein subunits, or the FERM domain of Fak. These interactions lead to conformational changes of Tec and translocation to the cytoplasmic membrane where, in a second step, Src kinases phosphorylate a conserved tyrosine residue in the catalytic domain thereby increasing Tec kinase activity. Autophosphorylation of a tyrosine residue in the SH3 domain further prevents the inhibitory intramolecular interaction resulting in a robust Tec kinase activation. [Pg.1261]

Hamada, K., Shimizu, T., Matsui, T., Tsukita, S., and Hakoshima, T., Structural basis of the membranetargeting and unmasking mechanisms of the radixin FERM domain, Embo J., 2000, 19, 4449. [Pg.344]

FERM FERM-domain (four-point-one ezrin, radixin, moesin)... [Pg.9]

Carver LA, Schnitzer JE (2003) Caveolae mining little caves for new cancer targets. Nat Rev Cancer 3 571-581 Ceccarelli DF, Song HK, Poy F et al (2006) Crystal structure of the FERM domain of focal adhesion kinase. J Biol Chem 281 252-259... [Pg.110]

FERM 4.1/ezrin/radixin/moesin domain Binding to cytoplasmic regions of transmembrane proteins... [Pg.1259]

C2, protein kinase C domain ENTH, epsin N-terminal homology FERM, band 4.1,exrin, radixin, moesin FYVE, Fabl, YOTB, Vacl, EEA1 MARCKS, myristoylated alanine-rich protein kinase C substrate PH, pleckstrin homology. [Pg.358]

Cohen LA, Guan JL. Residues within the first subdomain of the 63. FERM-like domain in focal adhesion kinase are important in its regulation. J. Biol. Chem. 2005 280 8197-8207. [Pg.781]


See other pages where FERM domain is mentioned: [Pg.974]    [Pg.1260]    [Pg.359]    [Pg.74]    [Pg.251]    [Pg.974]    [Pg.1260]    [Pg.220]    [Pg.228]    [Pg.775]    [Pg.350]    [Pg.186]    [Pg.231]    [Pg.413]    [Pg.104]    [Pg.32]    [Pg.33]    [Pg.974]    [Pg.1260]    [Pg.359]    [Pg.74]    [Pg.251]    [Pg.974]    [Pg.1260]    [Pg.220]    [Pg.228]    [Pg.775]    [Pg.350]    [Pg.186]    [Pg.231]    [Pg.413]    [Pg.104]    [Pg.32]    [Pg.33]    [Pg.417]    [Pg.516]    [Pg.238]    [Pg.246]    [Pg.137]    [Pg.104]    [Pg.411]   
See also in sourсe #XX -- [ Pg.326 ]




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