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Title: | Architecture of coatomer: Molecular characterization of delta-COP and protein interactions within the complex |
Authors: | Faulstich, D Auerbach, S Orci, L Ravazzola, M Wegchingel, S Lottspeich, F Stenbeck, G Harter, C Wieland, FT Tschochner, H |
Keywords: | ADP-ribosylation factor (ARF) |
Issue Date: | 1996 |
Publisher: | The Rockefeller University Press |
Citation: | The Journal of Cell Biology, 135(1): 53-61, 1996 |
Abstract: | Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles. In our attempt to analyze the physical and functional interactions between its seven subunits (coat proteins, [COPs] alpha-zeta), we engaged in a program to clone and characterize the individual coatomer subunits. We have now cloned, sequenced, and overexpressed bovine alpha-COP, the 135-kD subunit of coatomer as well as delta-COP, the 57-kD subunit and have identified a yeast homolog of delta-COP by cDNA sequence comparison and by NH2-terminal peptide sequencing. delta-COP shows homologies to subunits of the clathrin adaptor complexes AP1 and AP2. We show that in Golgi-enriched membrane fractions, the protein is predominantly found in COP I-coated transport vesicles and in the budding regions of the Golgi membranes. A knock-out of the delta-COP gene in yeast is lethal. Immunoprecipitation, as well as analysis exploiting the two-hybrid system in a complete COP screen, showed physical interactions between alpha- and epsilon-COPs and between beta- and delta-COPs. Moreover, the two-hybrid system indicates interactions between gamma- and zeta-COPs as well as between alpha- and beta' COPs. We propose that these interactions reflect in vivo associations of those subunits and thus play a functional role in the assembly of coatomer and/or serve to maintain the molecular architecture of the complex. |
Description: | Copyright © 2011 by The Rockefeller University Press. |
URI: | http://jcb.rupress.org/content/135/1/53 http://bura.brunel.ac.uk/handle/2438/5721 |
DOI: | http://dx.org.doi/10.1083/jcb.135.1.53 |
ISSN: | 0021-9525 |
Appears in Collections: | Biological Sciences Dept of Life Sciences Research Papers |
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