Title : Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in Saccharomyces cerevisiae.

Pub. Date : 2018 Aug 3

PMID : 29895620






3 Functional Relationships(s)
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1 Here, we report that Fpk1 mediates TORC2 signaling to control actin polarization, but not endocytosis, via aminophospholipid flippases. aminophospholipid serine/threonine protein kinase FPK1 Saccharomyces cerevisiae S288C
2 To search for specific targets of these flippase kinases, we exploited the fact that Fpk1 prefers to phosphorylate Ser residues within the sequence RXS(L/Y)(D/E), which is present ~90 times in the yeast proteome. Serine serine/threonine protein kinase FPK1 Saccharomyces cerevisiae S288C
3 Using a potent ATP-competitive small molecule, CMB4563, to preferentially inhibit TORC2, we found that Fpk1-mediated Akl1 phosphorylation inhibits Akl1 activity, which, in turn, reduces phosphorylation of Pan1 and of other endocytic coat proteins and ultimately contributes to a slowing of endocytosis kinetics. Adenosine Triphosphate serine/threonine protein kinase FPK1 Saccharomyces cerevisiae S288C