SGD Paper 
Deng Y, et al. (2009) A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor. EMBO Rep 10(1):58-64
Abstract: Arf (ADP-ribosylation factor) family small G proteins are crucial regulators of intracellular transport. The active GTP-bound form of Arf interacts with a set of proteins--effectors--which mediate the downstream signalling events of Arf activation. A well-studied class of Arf1 effectors comprises the coat complexes, such as the cis-Golgi-localized COPI (coat protein complex I) coat, and trans-Golgi network-endosomal clathrin coats. At least five different coats require Arf1-GTP to localize to organelle membranes. How a single Arf protein recruits different coat complexes to distinct membrane sites raises the question of how specificity is achieved. Here, we propose a molecular mechanism of this specificity for the COPI coat by showing a direct and specific interaction between a COPI subunit and a cis-Golgi localized subfamily of Arf guanine nucleotide exchange factors (GEFs) that takes place independently of Arf1 activation. In this way, a specific output on Arf1 activation can be programmed before the exchange reaction by the GEF itself.
| Status: Published | Type: Journal Article | Research Support, N.I.H., Intramural | Research Support, Non-U.S. Gov't | PubMed ID: 19039328 |
Topics addressed in this paper
Number of different genes curated to this paper: 4
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