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Titolo:
Major vault protein is a substrate of endogenous protein kinases in CHO and PC12 cells
Autore:
Ehrnsperger, C; Volknandt, W;
Indirizzi:
Univ Frankfurt, AK Neurochem, Biozentrum, D-60439 Frankfurt, Germany Univ Frankfurt Frankfurt Germany D-60439 rum, D-60439 Frankfurt, Germany
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 10, volume: 382, anno: 2001,
pagine: 1463 - 1471
SICI:
1431-6730(200110)382:10<1463:MVPIAS>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESISTANCE-RELATED PROTEIN; INHIBITOR GF 109203X; RIBONUCLEOPROTEIN-PARTICLES; CASEIN KINASE; ELECTRIC RAY; CANCER CELL; MULTIDRUG-RESISTANCE; SYNAPTIC VESICLES; DRUG RESISTANCE; DEGRADATION;
Keywords:
casein kinase II; phosphoprotein; protein kinase C; protein kinase inhibitor; protein tyrosine kinase; vault;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Volknandt, W Univ Frankfurt, AK Neurochem, Biozentrum, Marie Curie Str 9, D-60439 Frankfurt, Germany Univ Frankfurt Marie Curie Str 9 Frankfurt Germany D-60439 y
Citazione:
C. Ehrnsperger e W. Volknandt, "Major vault protein is a substrate of endogenous protein kinases in CHO and PC12 cells", BIOL CHEM, 382(10), 2001, pp. 1463-1471

Abstract

Major vault protein (MVP) is the predominant member of a large cytosolic ribonucleoprotein particle, termed vault. We have previously shown that MVP derived from electric ray electric organ becomes phosphorylated by protein kinase C in vitro and by tyrosine kinase in vivo. Here we show that MVP from two mammalian cell lines (CHO and PC12 cell) becomes highly phosphorylated by endogenous protein kinases in cell-free systems. The susceptibility, to protein kinases differs substantially from those observed in MVP derived from electric organ. Phosphorylation of MVP depends on the presence of Mg2and can be inhibited by the chelating agent EDTA. Inhibitors of casein kinase II attenuate the phosphorylation of MVP. In contrast to CHO cells, addition of recombinant casein kinase II enhances the phosphorylation of MVP inPC12 cells. Endogenous kinase activity is of particulate nature and copurifies with vault particles. Immuno-affinity purified vaults containing recombinant tagged MVP expressed in CHO cells reveal no autophosphorylation, suggesting that protein kinase activity is not an intrinsic property of vaults. Our results suggest that cell-specific phosphorylation of MVP may play a critical role in vault function.

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Documento generato il 04/04/20 alle ore 22:41:32