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Titolo:
Mammalian homologues of yeast Sec31p - An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport
Autore:
Tang, BL; Zhang, T; Low, DYH; Wong, ET; Horstmann, H; Hong, WJ;
Indirizzi:
Inst Mol & Cell Biol, Membrane Biol Lab, Singapore 117609, Singapore Inst Mol & Cell Biol Singapore Singapore 117609 gapore 117609, Singapore
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 18, volume: 275, anno: 2000,
pagine: 13597 - 13604
SICI:
0021-9258(20000505)275:18<13597:MHOYS->2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TRANSPORT; INTERMEDIATE COMPARTMENT; SUBUNIT INTERACTIONS; VESICLE FORMATION; SEC13P COMPLEX; COAT PROTEINS; COPII; SEC24P; RECONSTITUTION; APPARATUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Tang, BL Inst Mol & Cell Biol, Membrane Biol Lab, 30 Med Dr, Singapore 117609, Singapore Inst Mol & Cell Biol 30 Med Dr Singapore Singapore 117609 gapore
Citazione:
B.L. Tang et al., "Mammalian homologues of yeast Sec31p - An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport", J BIOL CHEM, 275(18), 2000, pp. 13597-13604

Abstract

The yeast coat protein II (COPII) is responsible for vesicle budding from the endoplasmic reticulum (ER), Mammalian functional homologues for all yeast COPII components, except for Sec31p, have been reported. We have cloned a mammalian cDNA whose product (Sec31A) is about 26% identical to Saccharomyces cerevisiae Sec31p, Data base searches also revealed another partial sequence encoding a polypeptide (Sec31B) that is 40% identical to Sec31A Northern analysis revealed that Sec31A transcripts are ubiquitously and abundantly expressed, while Sec31B transcripts are particularly enriched in the testis and thymus, but present in very low levels in other tissues. Sec31A islocalized to vesicular structures that scatter throughout the cell but areconcentrated at the perinuclear region. The structures marked by Sec31A contain Sec13, a component of COPII that is well characterized to mark the ERexit sites. Immunoelectron microscopy revealed that Sec31A colocalizes with Sec13 in structures with extensive vesicular-tubular profiles. Antibodiesraised against a C-terminal portion of Sec31A co-precipitate Sec13 and inhibit ER-Golgi transport of temperature-arrested vesicular stomatitis G protein in a semi-intact cell assay. Cytosol immunodepleted of Sec31A failed tosupport vesicular stomatitis G protein transport, which can be rescued by a high molecular weight fraction of the cytosol containing both Sec31A and Sec13, We conclude that Sec31A represents a functional mammalian homologue of yeast Sec31p.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 19:27:48