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DC Field | Value | Language |
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dc.contributor.author | Faulstich, D | - |
dc.contributor.author | Auerbach, S | - |
dc.contributor.author | Orci, L | - |
dc.contributor.author | Ravazzola, M | - |
dc.contributor.author | Wegchingel, S | - |
dc.contributor.author | Lottspeich, F | - |
dc.contributor.author | Stenbeck, G | - |
dc.contributor.author | Harter, C | - |
dc.contributor.author | Wieland, FT | - |
dc.contributor.author | Tschochner, H | - |
dc.date.accessioned | 2011-07-29T20:11:08Z | - |
dc.date.available | 2011-07-29T20:11:08Z | - |
dc.date.issued | 1996 | - |
dc.identifier.citation | The Journal of Cell Biology, 135(1): 53-61, 1996 | en_US |
dc.identifier.issn | 0021-9525 | - |
dc.identifier.uri | http://jcb.rupress.org/content/135/1/53 | en |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/5721 | - |
dc.description | Copyright © 2011 by The Rockefeller University Press. | en_US |
dc.description.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. | en_US |
dc.description.sponsorship | This work was supported by The Deutsche Forschungsgemeinschaft (SFB 352), the Human Frontier Science Program, and the Swiss National Science Foundation No. 31-43366.95. | en_US |
dc.language.iso | en | en_US |
dc.publisher | The Rockefeller University Press | en_US |
dc.subject | ADP-ribosylation factor (ARF) | en_US |
dc.title | Architecture of coatomer: Molecular characterization of delta-COP and protein interactions within the complex | en_US |
dc.type | Research Paper | en_US |
dc.identifier.doi | http://dx.org.doi/10.1083/jcb.135.1.53 | - |
Appears in Collections: | Biological Sciences Dept of Life Sciences Research Papers |
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