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Vol. 11, Issue 7, 2251-2265, July 2000
Michigan State University-Department of Energy Plant Research
Laboratory, Michigan State University, East Lansing, Michigan
48824-1312
The Sec1p family of proteins are thought to be involved in the
regulation of vesicle fusion reactions through interaction with
t-SNAREs (target soluble N-ethylmaleimide-sensitive
factor attachment protein receptors) at the target membrane. AtVPS45 is
a member of this family from Arabidopsis thaliana that
we now demonstrate to be present on the trans-Golgi
network (TGN), where it colocalizes with the vacuolar cargo receptor
AtELP. Unlike yeast Vps45p, AtVPS45 does not interact with, or
colocalize with, the prevacuolar t-SNARE AtPEP12. Instead, AtVPS45
interacts with two t-SNAREs, AtTLG2a and AtTLG2b, that show similarity
to the yeast t-SNARE Tlg2p. AtTLG2a and -b each colocalize with AtVPS45 at the TGN; however, AtTLG2a is in a different region of the TGN than
AtTLG2b by immunogold electron microscopy. Therefore, we propose that
complexes containing AtVPS45 and either AtTLG2a or -b define functional
subdomains of the TGN and may be required for different trafficking
events. Among other Arabidopsis SNAREs, AtVPS45
antibodies preferentially coprecipitate AtVTI1b over the closely
related isoform AtVTI1a, implying that AtVTI1a and AtVTI1b also have
distinct functions within the cell. These data point to a functional
complexity within the plant secretory pathway, where proteins encoded
by gene families have specialized functions, rather than functional redundancy.
Corresponding author. E-mail address:
nraikhel{at}pilot.msu.edu.
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