Fig. 3. Composition of proposed tethering complexes. For each complex the known
components in the yeast S. cerevisiae are shown, arranged by size,
and identifiable domains indicated. In each case the standard gene name in the
Saccharomyces Genome Database is given first, followed by alternative
names that have also been used in recent publications. Vps51p is encoded by
the open reading frame YKR020w (Elizabeth Conibear, personal
communication). The two sets of related subunits of the TRAPP complexes are
indicated by different colours. Homologues of most of these proteins exist in
higher eukaryotes, but in some cases have extra domains. Thus in mammals Sec5
has an N-terminal TIG domain, Exo84 a PH domain, Vam6 a CNH domain
(Caplan et al., 2001) and Vam2
a C-terminal RING-H2 domain (Radisky et
al., 1997). Vps54 has an N-terminal zinc-finger-like domain in
Drosophila and C. elegans, but not in mammals. Vam6 in both
yeast and higher eukaryotes has a conserved half RING domain (C2HC) at its
C-terminus. The `p' has been removed from the yeast protein names for
clarity.
