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Titolo:
P125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins
Autore:
Tani, K; Mizoguchi, T; Iwamatsu, A; Hatsuzawa, K; Tagaya, M;
Indirizzi:
Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 1920392, Japan Tokyo UnivPharm & Life Sci Tokyo Japan 1920392 ci, Tokyo 1920392, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanagawa 2360004, Japan KirinBrewery Co Ltd Kanagawa Japan 2360004 nol, Kanagawa 2360004, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 29, volume: 274, anno: 1999,
pagine: 20505 - 20512
SICI:
0021-9258(19990716)274:29<20505:PIANMS>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION FACTOR; ENDOPLASMIC-RETICULUM; GOLGI-APPARATUS; TRANSPORT VESICLES; CIS-GOLGI; INTERMEDIATE COMPARTMENT; SUBUNIT INTERACTIONS; COATED VESICLES; BETA-COP; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Tagaya, M Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 1920392, Japan Tokyo Univ Pharm & Life Sci Tokyo Japan 1920392 1920392, Japan
Citazione:
K. Tani et al., "P125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins", J BIOL CHEM, 274(29), 1999, pp. 20505-20512

Abstract

COPII-coated vesicles are involved in protein transport from the endoplasmic reticulum to the Gels apparatus. COPII consists of three parts: Sar1p and the two protein complexes, Sec23p-Sec24p and Sec13p-Sec31p. Using a glutathione S-transferase fusion protein with mouse Sec23p, we identified a novel mammalian Sec23p-interacting protein, p125, which is clearly distinct from Sec24p. The N-terminal region of p125 is rich in proline residues, and the central and C-terminal regions exhibit significant homology to phospholipid-modifying proteins, especially phosphatidic acid preferring-phospholipase A(1). We transiently expressed p125 and mouse Sec23p in mammalian cells and examined their interaction. The results showed that the N-terminal region of p125 is important for the interaction with Sec23p, We confirmed the interaction between the two proteins by a yeast two-hybrid assay. Overexpression of p125, like that of mammalian Sec23p, caused disorganization of the endoplasmic reticulum-Golgi intermediate compartment and Gels apparatus, suggesting its role in the early secretory pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 03:03:43