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Titolo:
Sorting of furin at the trans-Golgi network - Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins
Autore:
Teuchert, M; Schafer, W; Berghofer, S; Hoflack, B; Klenk, HD; Garten, W;
Indirizzi:
Inst Pasteur, Inst Biol, EP 525, CNRS, F-59021 Lille, France Inst PasteurLille France F-59021 l, EP 525, CNRS, F-59021 Lille, France Univ Marburg, Inst Virol, D-35037 Marburg, Germany Univ Marburg Marburg Germany D-35037 nst Virol, D-35037 Marburg, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 274, anno: 1999,
pagine: 8199 - 8207
SICI:
0021-9258(19990319)274:12<8199:SOFATT>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
MANNOSE 6-PHOSPHATE RECEPTORS; KINASE-II PHOSPHORYLATION; CLATHRIN-ASSOCIATED PROTEINS; HIGH-AFFINITY INTERACTION; COATED VESICLES; CELL-SURFACE; INTRACELLULAR TRAFFICKING; PROPROTEIN CONVERTASE; INVITRO BINDING; MEDIUM CHAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Garten, W InstLille,ur, Inst Biol, EP 525, CNRS, BP 447,1 Rue Prof Calmette, F-59021 Inst Pasteur BP 447,1 Rue Prof Calmette Lille France F-59021 21
Citazione:
M. Teuchert et al., "Sorting of furin at the trans-Golgi network - Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins", J BIOL CHEM, 274(12), 1999, pp. 8199-8207

Abstract

The eukaryotic subtilisin-like endoprotease furin is found predominantly in the trans-Golgi network (TGN) and cycles between this compartment, the cell surface, and the endosomes. There is experimental evidence for endocytosis from the plasma membrane and transport from endosomes to the TGN, but direct exit from the TGN to endosomes via clathrin-coated vesicles has only been discussed but not directly shown so far. Here we present data showing that expression of furin promotes the first step of clathrin-coat assembly at the TGN, the recruitment of the Gels-specific assembly protein AP-I on Golgi membranes. Further, we report that furin indeed is present in isolated clathrin-coated vesicles, packaging into clathrin-coated vesicles requires signal components in the furin cytoplasmic domain which can be recognized by AP-1 assembly proteins. We found that besides depending on the phosphorylation state of a casein kinase II site, interaction of the furin tail with AP-1 and its mu 1subunit is mediated by a tyrosine motif and to less extentby a leucine-isoleucine signal, whereas a monophenylalanine motif is only involved in binding to the intact AP-1 complex. This study implies that high affinity interaction of AP-1 or mu 1 with the cytoplasmic tail of furin needs a complex interplay of signal components rather than one distinct signal.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 11:33:46