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001-es BibID:	BIBFORM028724
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases / Ferenc Erdődi, Enikő Kiss, Michael P. Walsh, Bjarki Stefansson, Jing Ti Deng, Masumi Eto, David L. Brautigan, David J. Hartshorne
Dátum:	2003
ISSN:	0006-291X
Megjegyzések:	Protein phosphatases play key roles in cellular regulation and are subjected to control by protein inhibitors whose activity is in turn regulated by phosphorylation. Here we investigated the possible regulation of phosphorylation-dependent type-1 protein phosphatase (PP1) inhibitors, CPI-17, PHI-1, and KEPI, by various kinases. Protein kinases A (PKA) and G (PKG) phosphorylated CPI-17 at the inhibitory site (T38), but not PHI-1 (T57). Phosphorylated CPI-17 inhibited the activity of both the PP1 catalytic subunit (PP1c) and the myosin phosphatase holoenzyme (MPH) with IC(50) values of 1-8 nM. PKA predominantly phosphorylated a site distinct from the inhibitory T73 in KEPI, whereas PKG was ineffective. Integrin-linked kinase phosphorylated KEPI (T73) and this dramatically increased inhibition of PP1c (IC(50)=0.1 nM) and MPH (IC(50)=8 nM). These results suggest that the regulatory phosphorylation of CPI-17 and KEPI may involve distinct kinases and signaling pathways.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Biochemical and Biophysical Research Communications. - 306 : 2 (2003), p. 382-387. -
További szerzők:	Kiss Enikő Walsh, Michael P. Stefansson, Bjarki Deng, Jing Ti Eto, Masumi Brautigan, David L. Hartshorne, David J.
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