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Vol. 13, Issue 11, 3761-3774, November 2002
MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, United
Kingdom
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 organization 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 article, we report the
characterization 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 Caenorhabditis 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. Herein, 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 Saccharomyces cerevisiae, which we call COY1. Deletion of COY1 does not affect
viability, but strikingly restores normal growth to cells lacking the
Golgi soluble N-ethylmaleimide-sensitive factor
attachment protein receptor 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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