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Originally published In Press as doi:10.1074/jbc.M006143200 on October 19, 2000

J. Biol. Chem., Vol. 276, Issue 7, 5152-5165, February 16, 2001
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Proteomics Characterization of Abundant Golgi Membrane Proteins*

Alexander W. BellDagger §, Malcolm A. Ward§, Walter P. Blackstock, Hamzah N. M. Freeman, Jyoti S. Choudhary, Alan P. Lewis, Dipti Chotai, Ali FazelDagger , Jennifer N. GushueDagger , Jacques Paiement||, Sandrine PalcyDagger , Eric ChevetDagger , Myriam Lafrenière-RoulaDagger , Roberto Solari, David Y. ThomasDagger , Adele Rowley, and John J. M. BergeronDagger **

From the Dagger  Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 2B2, Canada,  GlaxoWellcome Research and Development, Stevenage SG1 2NY, United Kingdom, and || Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montreal, Quebec H3T 1J4, Canada

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 Golgi 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 sequencing of proteins. Major membrane proteins corresponded to known Golgi residents, a Golgi lectin, anterograde cargo, and an abundance of trafficking proteins including KDEL receptors, p24 family members, SNAREs, Rabs, a single ARF-guanine nucleotide exchange factor, and two SCAMPs. Analytical fractionation and 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 2P24 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 Golgi 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.

* This work was supported by a Medical Research Council of Canada/Pharmaceutical Manufacturers Association of Canada grant (to J. J. M. B. and D. Y. T.) with GlaxoWellcome, Stevenage, UK and an MRC Genomics grant (to J. J. M. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ296152 and AJ296153.

§ Both authors contributed equally to this work and should be considered co-first authors.

** To whom correspondence should be addressed: Dept. of Anatomy and Cell Biology, McGill University, 3640 University St., Montreal, Quebec H3A 2B2, Canada. Fax: 514-398-5047; E-Mail: bergeron@med.mcgill.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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