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Structural organization and regulation of the guanine nucleotide exchange factor C3G

AutorCarabias, Arturo ; Gómez-Hernández, María ; Martín-Gracia, Beatriz; Guerrero Arroyo, María del Carmen ; Pereda, José M. de
Fecha de publicación2016
EditorSociedad Española de Bioquímica y Biología Molecular
CitaciónXXXIX Congreso SEBBM (2016)
ResumenC3G is a guanine nucleotide exchange factor (GEF) for some members of the Ras family of GTPases including Rap1 and R-Ras. C3G is involved in the regulation of a wide range of cellular processes such as proliferation, differentiation, cytoskeletal remodelling, transformation, and apoptosis. C3G (120 kDa) is a tripartite protein according to its structural and functional features: (i) The N-terminal part contains an α-helical rich region that binds to the cytoplasmic tail of E-cadherin. (ii) The central segment contains five Pro-rich sequences (P0-P4) that mediate binding to the SH3 domains of at least Crk, p130Cas, Grb2, Hck and c-Abl proteins. Furthermore Tyr 504 in this region is phosphorylated by Src-family kinases during activation of C3G. (iii) The GEF activity of C3G lies in the C-terminal third, which consists of a Ras Exchange Motif (REM) and a catalytic Cdc25H domain. Here we show that C3G adopts a closed conformation stabilized by a head-tail interaction. We have identified some residues involved in this intramolecular interaction. Other GEFs of the Cdc25H family are autoinhibited by analogous head-tail interactions. We are currently analyzing the relationship between the conformational state of C3G and its GEF activity. In this context we are also analyzing the effect of post-transductional modifications on the structural organization of C3G and its GEF catalytic activity.
DescripciónResumen del póster presentado al XXXIX Congreso de la Sociedad Española de Bioquímica y Biología Molecular, celebrado en Salamanca del 5 al 8 de septiembre de 2016.
URIhttp://hdl.handle.net/10261/169470
Aparece en las colecciones: (IBMCC) Comunicaciones congresos
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