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Titolo:
THE MAMMALIAN HOMOLOG OF YEAST SEC13P IS ENRICHED IN THE INTERMEDIATECOMPARTMENT AND IS ESSENTIAL FOR PROTEIN-TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-APPARATUS
Autore:
TANG BL; PETER F; KRIJNSELOCKER J; LOW SH; GRIFFITHS G; HONG WJ;
Indirizzi:
NATL UNIV SINGAPORE,INST MOL & CELL BIOL,MEMBRANE BIOL LAB,10 KENT RIDGE CRESCENT SINGAPORE 119260 SINGAPORE NATL UNIV SINGAPORE,INST MOL & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 119260 SINGAPORE EUROPEAN MOL BIOL LAB D-69012 HEIDELBERG GERMANY UNIV CALIF SAN FRANCISCO,DEPT ANAT SAN FRANCISCO CA 94143
Titolo Testata:
Molecular and cellular biology
fascicolo: 1, volume: 17, anno: 1997,
pagine: 256 - 266
SICI:
0270-7306(1997)17:1<256:TMHOYS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTP-BINDING PROTEIN; BREFELDIN-A; SECRETORY PATHWAY; CIS-GOLGI; BETA-COP; GUANINE-NUCLEOTIDE; COAT PROTEINS; MEMBRANE-GLYCOPROTEINS; PERMEABILIZED CELLS; ORGANELLE STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
68
Recensione:
Indirizzi per estratti:
Citazione:
B.L. Tang et al., "THE MAMMALIAN HOMOLOG OF YEAST SEC13P IS ENRICHED IN THE INTERMEDIATECOMPARTMENT AND IS ESSENTIAL FOR PROTEIN-TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-APPARATUS", Molecular and cellular biology, 17(1), 1997, pp. 256-266

Abstract

The role of COPII components in endoplasmic reticulum (ER)-Golgi transport, first identified in the yeast Saccharomyces cerevisiae, has yetto be fully characterized in higher eukaryotes. A human cDNA whose predicted amino acid sequence showed 70% similarity to the yeast Sec13p has previously been cloned. Antibodies raised against the human SEC13 protein (mSEC13) recognized a cellular protein of 35 kDa in both the soluble and membrane fractions. Like the yeast Sec13p, mSEC13 exist in the cytosol in both monomeric and higher-molecular-weight forms. Immunofluorescence microscopy localized mSEC13 to the characteristic spottyER-Golgi intermediate compartment (ERGIC) in cells of all species examined, where it colocalized well with the KDEL receptor, an ERGIC marker, at 15 degrees C. Immunoelectron microscopy also localized mSEC13 to membrane structures close to the Golgi apparatus. mSEC13 is essential for ER-to-Golgi transport, since both the His(6)-tagged mSEC13 recombinant protein and the affinity-purified mSEC13 antibody inhibited thetransport of restrictive temperature-arrested vesicular stomatitis virus G protein from the ER to the Golgi apparatus in a semi-intact cellassay. Moreover, cytosol immunodepleted of mSEC13 could no longer support ER-Golgi transport. Transport could be restored in a dose-dependent manner by a cytosol fraction enriched in the high-molecular-weight mSEC13 complex but not by a fraction enriched in either monomeric mSEC13 or recombinant mSEC13. As a putative component of the mammalian COPII complex, mSEC13 showed partially overlapping but mostly different properties in terms of localization, membrane recruitment, and dynamicscompared to that of beta-COP, a component of the COPI complex.

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Documento generato il 27/09/20 alle ore 05:17:12