A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding.
Open Access
- 1 December 1996
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 135 (5) , 1239-1248
- https://doi.org/10.1083/jcb.135.5.1239
Abstract
Formation of non-clathrin-coated vesicles requires the recruitment of several cytosolic factors to the Golgi membrane. To identify membrane proteins involved in this budding process, a highly abundant type I transmembrane protein (p23) was isolated from mammalian Golgi-derived COPI-coated vesicles, and its cDNA was cloned and sequenced. It belongs to the p24 family of proteins involved in the budding of transport vesicles (Stamnes, M.A., M.W. Craighead, M.H. Hoe, N. Lampen, S. Geromanos, P. Tempst, and J.E. Rothman. 1995. Proc. Natl. Acad. Sci. USA. 92:8011-8015). p23 consists of a large NH2-terminal luminal domain and a short COOH-terminal cytoplasmic tail (-LRRFFKAKKLIE-CO2-) that shows similarity, but not identity, with the sequence motif-KKXX-CO2-, known as a signal for retrieval of escaped ER-resident membrane proteins (Jackson, M.R., T. Nilsson, and P.A. Peterson. 1990. EMBO (Eur. Mol. Biol. Organ.) J. 9:3153-3162; Nilsson, T., M. Jackson, and P.A. Peterson. 1989. Cell. 58:707-718). The cytoplasmic tail of p23 binds to coatomer with similar efficiency as known KKXX motifs. However, the p23 tail differs from the KKXX motif in having an additional motif needed for binding of coatomer. p23 is localized to Golgi cisternae and, during vesicle formation, it concentrates into COPI-coated buds and vesicles. Biochemical analysis revealed that p23 is enriched in vesicles by a factor of approximately 20, as compared with the donor Golgi fraction, and is present in amounts stoichiometric to the small GTP-binding protein ADP-ribosylation factor (ARF) and coatomer. From these data we conclude that p23 represents a Golgi-specific receptor for coatomer involved in the formation of COPI-coated vesicles.Keywords
This publication has 52 references indexed in Scilit:
- Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulumPublished by Elsevier ,1994
- About turn for the COPs?Cell, 1994
- Mechanisms of intracellular protein transportNature, 1994
- Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulumCell, 1994
- ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding proteinCell, 1991
- A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptinNature, 1991
- Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulumCell, 1989
- Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stackCell, 1989
- A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stackCell, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970