Abstract
Phosducin-like Protein Regulates G-Protein βγ Folding by Interaction with Tailless Complex Polypeptide-1α: DEPHOSPHORYLATION OR SPLICING OF PhLP TURNS THE SWITCH TOWARD REGULATION OF Gβγ FOLDING
Highlights
Phosducin-like protein (PhLP) exists in two splice variants PhLPLONG (PhLPL) and PhLPSHORT (PhLPS)
PhLPS and several truncated mutants of PhLPS interacted with the subunit tailless complex polypeptide-1␣ (TCP-1␣) of the CCT chaperonin complex, which is involved in protein folding
Effects of Phosphorylation of PhLPL by casein kinase 2 (CK2) on G␥ Binding—We have recently demonstrated that PhLPL is constitutively phosphorylated by CK2 and that this phosphorylation inhibited the effect of PhLP on G␥-mediated inositol phosphate generation in intact HEK 293 cells [12]
Summary
Phosducin-like protein (PhLP) exists in two splice variants PhLPLONG (PhLPL) and PhLPSHORT (PhLPS). We report here that inhibition of G␥ signaling in intact HEK cells by PhLPS was independent of direct G␥ binding; PhLPS caused down-regulation of G and G␥ proteins. We recently demonstrated that PhLPS showed a more pronounced G␥ inhibition than PhLPL in transiently transfected HEK 293 cells [12].
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