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Titolo:
CHARACTERIZATION OF PHOSPHORYLATION SITES IN THE CYTOPLASMIC DOMAIN OF THE 300 KDA MANNOSE-6-PHOSPHATE RECEPTOR
Autore:
ROSORIUS O; MIESKES G; ISSINGER OG; KORNER C; SCHMIDT B; VONFIGURA K; BRAULKE T;
Indirizzi:
UNIV GOTTINGEN,INST BIOCHEM 2 W-3400 GOTTINGEN GERMANY UNIV GOTTINGEN,INST BIOCHEM 2 W-3400 GOTTINGEN GERMANY UNIV GOTTINGEN,DEPT CLIN BIOCHEM W-3400 GOTTINGEN GERMANY UNIV SAARLAND,INST HUMAN GENET W-6650 HOMBURG GERMANY
Titolo Testata:
Biochemical journal
, volume: 292, anno: 1993,
parte:, 3
pagine: 833 - 838
SICI:
0264-6021(1993)292:<833:COPSIT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH FACTOR-II; MANNOSE 6-PHOSPHATE RECEPTOR; CASEIN KINASE-II; GLYCOGEN-SYNTHASE KINASE; RABBIT SKELETAL-MUSCLE; PROTEIN-KINASE; PHORBOL ESTER; BINDING; CELLS; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
O. Rosorius et al., "CHARACTERIZATION OF PHOSPHORYLATION SITES IN THE CYTOPLASMIC DOMAIN OF THE 300 KDA MANNOSE-6-PHOSPHATE RECEPTOR", Biochemical journal, 292, 1993, pp. 833-838

Abstract

The human 300 kDa mannose-6-phosphate receptor (MPR 300) is phosphorylated in vivo at serine residues of its cytoplasmic domain. Two-dimensional separation can resolve tryptic phosphopeptides into four major species. To identify the kinases involved in MPR 300 phosphorylation and the phosphorylation sites the entire coding sequence of the cytoplasmic tail was expressed in Escherichia coli. The isolated cytoplasmic domain was used as a substrate for four purified serine/threonine kinases [casein kinase II (CK II), protein kinase A (PKA), protein kinase Cand Ca2+/calmodulin kinase]. All kinases phosphorylate the cytoplasmic tail exclusively on serine residues. Inhibition studies using synthetic peptides, partial sequencing of isolated tryptic phosphopeptides and co-migration with tryptic phosphopeptides from MPR 300 labelled in vivo showed that (i) PKA phosphorylates the cytoplasmic MPR 300 domainat Ser20 and at a non-identified site, neither of which are phosphorylated in vivo, and that (ii) the two sites phosphorylated by CK II in vivo and in vitro are Ser82 and Ser157. The results indicate that the human MPR 300 is a physiological substrate of either CK II or a related kinase which may play a role in the transport function of MPR 300 and/or interaction with other proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 11:05:56