Bimodal interaction of coatomer with the p24 family of putative cargo receptors Journal Article

  

Authors:	Fiedler, K.; Veit, M.; Stamnes, M. A.; Rothman, J. E.
Article Title:	Bimodal interaction of coatomer with the p24 family of putative cargo receptors
Abstract:	Cytoplasmic domains of members of the p24 family of putative cargo receptors were shown to bind to coatomer, the coat protein of COPI-coated transport vesicles. Domains that contained dilysine endoplasmic reticulum retrieval signals bound the α-, β'-, and ε-COP subunits of coatomer, whereas other p24 domains bound the β-, γ-, and ζ-COP subunits and required a phenylalanine-containing motif. Transit of a CD8-p24 chimera from the endoplasmic reticulum through the Golgi complex was slowed when the phenylalanine motif was mutated, suggesting that this motif may function as an anterograde transport signal. The either-or bimodal binding of coatomer to p24 tails suggests models for how coatomer can potentially package retrograde-directed and anterograde-directed cargo into distinct COPI-coated vesicles.
Keywords:	nonhuman; protein domain; protein analysis; animals; membrane proteins; endoplasmic reticulum; amino acid sequence; molecular sequence data; recombinant fusion proteins; carrier proteins; cell membrane; biological transport; lysine; phenylalanine; golgi complex; cho cells; cricetinae; coatomer protein; nuclear envelope; coated vesicles; membrane receptor; golgi apparatus; human; priority journal; article; antigen p24
Journal Title:	Science
Volume:	273
Issue:	5280
ISSN:	0036-8075
Publisher:	American Association for the Advancement of Science
Date Published:	1996-09-06
Start Page:	1396
End Page:	1399
Language:	English
PUBMED:	8703076
PROVIDER:	scopus
DOI:	10.1126/science.273.5280.1396
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029796074&partnerID=40&md5=1c4a6df1a67166e898d445b32828218e
Notes:	Article -- Export Date: 22 November 2017 -- Source: Scopus

https://synapse.mskcc.org/synapse/works/has_related_data_chk/119395