Title : Phosphorylation of Cdc42 effector protein-4 (CEP4) by protein kinase C promotes motility of human breast cells.

Pub. Date : 2014 Sep 12

PMID : 25086031






5 Functional Relationships(s)
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Protein Name
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1 Single site mutants at Ser residues embedded in potential PKC consensus sites (Ser(18), Ser(77), Ser(80), and Ser(86)) were individually replaced with Asp residues to simulate phosphorylation. Serine protein kinase C alpha Homo sapiens
2 MS/MS analysis verified that Ser(18) and Ser(80) were directly phosphorylated by PKCalpha in vitro. Serine protein kinase C alpha Homo sapiens
3 MS/MS analysis verified that Ser(18) and Ser(80) were directly phosphorylated by PKCalpha in vitro. Serine protein kinase C alpha Homo sapiens
4 These findings support a model in which PKC-mediated phosphorylation of CEP4 at Ser(18) and Ser(80) causes its dissociation from Cdc42, thereby increasing its affinity for TEM4 and producing Rac activation, filopodium formation, and cell motility. Serine protein kinase C alpha Homo sapiens
5 These findings support a model in which PKC-mediated phosphorylation of CEP4 at Ser(18) and Ser(80) causes its dissociation from Cdc42, thereby increasing its affinity for TEM4 and producing Rac activation, filopodium formation, and cell motility. Serine protein kinase C alpha Homo sapiens