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Titolo:
PHOSPHORYLATION OF THE CYTOPLASMIC TAIL OF THE 300-KDA MANNOSE 6-PHOSPHATE RECEPTOR IS REQUIRED FOR THE INTERACTION WITH A CYTOSOLIC PROTEIN
Autore:
ROSORIUS O; ISSINGER OG; BRAULKE T;
Indirizzi:
UNIV GOTTINGEN,INST BIOCHEM 2,GOSSLERSTR 12D D-37073 GOTTINGEN GERMANY UNIV GOTTINGEN,INST BIOCHEM 2,GOSSLERSTR 12D D-37073 GOTTINGEN GERMANY UNIV SAARLAND,INST HUMAN GENET D-66421 HOMBURG GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 29, volume: 268, anno: 1993,
pagine: 21470 - 21473
SICI:
0021-9258(1993)268:29<21470:POTCTO>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR-II RECEPTOR; GOLGI;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
14
Recensione:
Indirizzi per estratti:
Citazione:
O. Rosorius et al., "PHOSPHORYLATION OF THE CYTOPLASMIC TAIL OF THE 300-KDA MANNOSE 6-PHOSPHATE RECEPTOR IS REQUIRED FOR THE INTERACTION WITH A CYTOSOLIC PROTEIN", The Journal of biological chemistry, 268(29), 1993, pp. 21470-21473

Abstract

The cytoplasmic tail of the human 300-kDa mannose 6-phosphate receptor (MPR 300-CT) is an excellent substrate for casein kinase II in vitro. The phosphorylated MPR 300-CT was cross-linked by means of bis(sulfosuccinimidyl) suberate mainly to a cytosolic protein of 35 kDa (referred to as TIP 35) and to 35- and 91-kDa proteins salt-washed from bovine brain membranes. Gel filtration suggested that TIP 35 is part of a higher molecular mass complex of approximately 130-150 kDa. Inhibition studies, using non-phosphorylated and phosphorylated MPR 300-CT and cross-linking, indicate that the interaction with TIP 35 is phosphorylation-specific. Furthermore, TIP 35 was only cross-linked to the MPR 300-CT phosphorylated by casein kinase II whereas the MPR 300-CT phosphorylated by protein kinase A failed to cross-link to TIP 35. These results indicate that the cytoplasmic tail of the MPR 300 interacts with a cytosolic protein depending on the phosphorylation by a casein kinase II-like kinase. The cross-linking with salt-washed membrane proteins, however, is inhibited by non-phosphorylated MPR 300-CT, suggesting that different structural determinants in the MPR 300-CT interact with cytosol- and membrane-derived proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 10:54:21