Sorting determinants in the transmembrane domain of p24 proteins Journal Article

  


Authors: Fiedler, K.; Rothman, J. E.
Article Title: Sorting determinants in the transmembrane domain of p24 proteins
Abstract: Members of the p24 family of putative cargo receptors are proposed to contain retrograde and anterograde trafficking signals in their cytoplasmic domain to facilitate coat protein binding and cycling in the secretory pathway. We have analyzed the role of the transmembrane domain (TMD) of a p24 protein isolated from COPI-coated intra-Golgi transport vesicles. CD8-p24 chimeras were transiently expressed in COS7 cells and analyzed by immunofluorescence and pulse-chase experiments. The localization and transit of the wild-type chimera from the endoplasmic reticulum (ER) through the Golgi complex involved a glutamic acid residue and a conserved glutamine in the TMD. The TMD glutamic acid mediated the localization of the chimeras to the ER in the absence of the conserved glutamine. Efficient ER exit required the TMD glutamine and was further facilitated by a pair of phenylalanine residues in the cytoplasmic tail. TMD residues of p24 proteins may mediate the interaction with integral membrane proteins of the vesicle budding machinery to ensure p24 packaging into transport vesicles.
Keywords: signal transduction; human cell; nonhuman; protein domain; animal cell; animals; protein targeting; membrane proteins; transfection; cos cells; animalia; endoplasmic reticulum; amino acid sequence; conserved sequence; molecular sequence data; sequence homology, amino acid; kinetics; recombinant fusion proteins; antigens, cd; glutamic acid; glutamine; phenylalanine; membrane binding; protein isolation; receptors, cell surface; antigens, cd8; golgi complex; membrane vesicle; coatomer protein; gag protein; golgi apparatus; humans; human; priority journal; article
Journal Title: Journal of Biological Chemistry
Volume: 272
Issue: 40
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1997-10-03
Start Page: 24739
End Page: 24742
Language: English
DOI: 10.1074/jbc.272.40.24739
PUBMED: 9312065
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030779039&doi=10.1074%2fjbc.272.40.24739&partnerID=40&md5=9f0bfafa8b48d9eaff8935e681b26636
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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MSK Authors
  1. James E Rothman
    120 Rothman
  2. Klaus M Fiedler
    6 Fiedler
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