Title : Serine phosphorylation differentially affects RhoA binding to effectors: implications to NGF-induced neurite outgrowth.

Pub. Date : 2006 May

PMID : 16109481






4 Functional Relationships(s)
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1 According to the molecular switch hypothesis of GTPase function GTP-loading of RhoA should be sufficient to activate its effectors uniformly. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
2 However, when monitoring NGF-induced binding of GTP-RhoA to multiple targets, we noted differential interactions with its effectors. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
3 Therefore, phosphorylation of serine(188) may serve as a novel secondary switch of RhoA capable of overriding GTP-binding-elicited effector activation to a subset of targets such as ROK, which interact with the C-terminus of RhoA. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
4 Therefore, phosphorylation of serine(188) may serve as a novel secondary switch of RhoA capable of overriding GTP-binding-elicited effector activation to a subset of targets such as ROK, which interact with the C-terminus of RhoA. Guanosine Triphosphate ras homolog family member A Rattus norvegicus