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A more recent version of this article appeared on November 1, 2002
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Submitted on June 18, 2002
Revised on July 31, 2002
Accepted on August 8, 2002
1 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
* Corresponding author. E-mail address: sean{at}mrc-lmb.cam.ac.uk.
Large coiled-coil proteins are being found in increasing numbers on the membranes of the Golgi apparatus, and have been proposed to function in tethering of transport vesicles and in the organisation of the Golgi stack. Members of one class of Golgi coiled-coil protein, comprising giantin and golgin-84, are anchored to the bilayer by a single C-terminal transmembrane domain (TMD). In this paper we report the characterisation of another mammalian coiled-coil protein, CASP, that was originally identified as an alternatively spliced product of the CUTL1 gene that encodes CCAAT-displacement protein (CDP), the human homologue of the Drosophila homeodomain protein Cut. We find that the C. elegans homologues of CDP and CASP are also generated from a single gene. CASP lacks the DNA binding motifs of CDP, and was previously reported to be a nuclear protein. Here we show that it is in fact a Golgi protein with a C-terminal TMD, and shares with giantin and golgin-84 a conserved histidine in its TMD. However, unlike these proteins, CASP has a homologue in S. cerevisiae, which we call COY1. Deletion of COY1 does not affect viability, but strikingly restores normal growth to cells lacking the Golgi SNARE Gos1p. The conserved histidine is necessary for Coy1p's activity in cells lacking Gos1p, suggesting that the TMD of these transmembrane Golgi coiled-coil proteins is directly involved in their function.
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