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Titolo:
Proteomics characterization of abundant Golgi membrane proteins
Autore:
Bell, AW; Ward, MA; Blackstock, WP; Freeman, HNM; Choudhary, JS; Lewis, AP; Chotai, D; Fazel, A; Gushue, JN; Paiement, J; Palcy, S; Chevet, E; Lafreniere-Roula, M; Solari, R; Thomas, DY; Rowley, A; Bergeron, JJM;
Indirizzi:
McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 2B2, Canada McGill Univ Montreal PQ Canada H3A 2B2 Biol, Montreal, PQ H3A 2B2, Canada Glaxo Wellcome Res & Dev Ltd, Stevenage SG1 2NY, Herts, England Glaxo Wellcome Res & Dev Ltd Stevenage Herts England SG1 2NY rts, England Univ Montreal, Dept Pathol & Biol Cellulaire, Montreal, PQ H3T 1J4, CanadaUniv Montreal Montreal PQ Canada H3T 1J4 re, Montreal, PQ H3T 1J4, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 7, volume: 276, anno: 2001,
pagine: 5152 - 5165
SICI:
0021-9258(20010216)276:7<5152:PCOAGM>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE-EXCHANGE PROTEIN; ENDOPLASMIC-RETICULUM; BREFELDIN-A; VESICULAR TRANSPORT; VESICLE TRANSPORT; MASS-SPECTROMETRY; PLASMA-MEMBRANE; MEDIAL GOLGI; SEQUENCE; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
79
Recensione:
Indirizzi per estratti:
Indirizzo: Bergeron, JJM McGill Univ, Dept Anat & Cell Biol, 3640 Univ St, Montreal, PQ H3A 2B2, Canada McGill Univ 3640 Univ St Montreal PQ Canada H3A 2B2 , Canada
Citazione:
A.W. Bell et al., "Proteomics characterization of abundant Golgi membrane proteins", J BIOL CHEM, 276(7), 2001, pp. 5152-5165

Abstract

A mass spectrometric analysis of proteins partitioning into Triton X-114 from purified hepatic Golgi apparatus (84% purity by morphometry, 122-fold enrichment over the homogenate for the Gels marker galactosyl transferase) led to the unambiguous identification of 81 proteins including a novel Golgi-associated protein of 34 kDa (GPP34), The membrane protein complement was resolved by SDS-polyacrylamide gel electrophoresis and subjected to a hierarchical approach using delayed extraction matrix-assisted laser desorption ionization mass spectrometry characterization by peptide mass fingerprinting, tandem mass spectrometry to generate sequence tags, and Edman sequencingof proteins. Major membrane proteins corresponded to known Gels residents,a Gels lectin, anterograde cargo, and an abundance of trafficking proteinsincluding KDEL receptors, p24 family members, SNAREs, Rabs, a single ARF-guanine nucleotide exchange factor, and two SCAMPs. Analytical fractionationand gold immunolabeling of proteins in the purified Golgi fraction were used to assess the intra-Golgi and total cellular distribution of GPP34, two SNAREs, SCAMPs, and the trafficking proteins GBF1, BAP31, and alpha (2)P24 identified by the proteomics approach as well as the endoplasmic reticulum contaminant calnexin, Although GPP34 has never previously been identified as a protein, the localization of GPP34 to the Gels complex, the conservation of GPP34 from yeast to humans, and the cytosolically exposed location of GPP34 predict a role for a novel coat protein in Golgi trafficking.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:11:28