Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPII
Autore:
Tang, BL; Ong, YS; Huang, B; Wei, S; Wong, ET; Qi, R; Horstmann, H; Hong, W;
Indirizzi:
Inst Mol & Cell Biol, Membrane Biol Lab, Singapore 117609, Singapore Inst Mol & Cell Biol Singapore Singapore 117609 gapore 117609, Singapore Inst Mol & Cell Biol, Cent Imaging & Histol Facil, Singapore 117609, Singapore Inst Mol & Cell Biol Singapore Singapore 117609 gapore 117609, Singapore Inst Mol & Cell Biol, Microsequencing Lab, Singapore 117609, Singapore Inst Mol & Cell Biol Singapore Singapore 117609 gapore 117609, Singapore
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 43, volume: 276, anno: 2001,
pagine: 40008 - 40017
SICI:
0021-9258(20011026)276:43<40008:AMPEIE>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TO-GOLGI TRANSPORT; MAMMALIAN KDEL RECEPTOR; RAB GTPASES; SUBUNIT INTERACTIONS; COAT PROTEINS; LIVING CELLS; YEAST SEC24P; BREFELDIN-A; BETA-COP; ER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
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., "A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPII", J BIOL CHEM, 276(43), 2001, pp. 40008-40017

Abstract

Although all mammalian COPII components have now been cloned, little is known of their interactions with other regulatory proteins involved in exit from the endoplasmic reticulum (ER). We report here that a mammalian protein(Yip1A) that is about 31% identical to S. cerevisiae and which interacts with and modulates COPII-mediated ER-Golgi transport. Yip1A transcripts are ubiquitously expressed. Transcripts of a related mammalian homologue, Yip1B, are found specifically in the heart. Indirect immunofluorescence microscopy revealed that Yip1A is localized to vesicular structures that are concentrated at the perinuclear region. The structures marked by Yip1A co-localized with Sec31A and Sec13, components of the COPII coat protein complex. Immunoelectron microscopy also showed that Yip1A co-localizes with Sec13 at ERexit sites. Overexpression of the hydrophilic N terminus of Yip1A arrests ER-Golgi transport of the vesicular stomatitis G protein and causes fragmentation and dispersion of the Golgi apparatus. A glutathione S-transferase fusion protein with the hydrophilic N terminus of Yip1A (GST-Yip1A) is able to bind to and deplete vital components from rat liver cytosol that is essential for in. vitro vesicular stomatitis G transport. Peptide sequence analysis of cytosolic proteins that are specifically bound to GST-Yip1A revealed, among other proteins, mammalian COPII components Sec23 and Sec24. A highly conserved domain at the N terminus of Yip1A is required for Sec23/Sec24 interaction. Our results suggest that Yip1A is involved in the regulation of ER-Golgi traffic at the level of ER exit sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/10/20 alle ore 01:15:50