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Vol. 13, Issue 10, 3493-3507, October 2002
and
*Membrane Biology Laboratory, Institute of Molecular and Cell
Biology, Singapore 117609, Singapore; The subcellular localization, interacting partners, and function of
GS15, a Golgi SNARE, remain to be established. In our present study, it
is revealed that unlike proteins (Bet1 and the KDEL receptor) cycling
between the Golgi and the intermediate compartment (IC, inclusive of
the ER exit sites), GS15 is not redistributed into the IC upon
incubation at 15°C or when cells are treated with brefeldin A. Immuno-electron microscopy (immuno-EM) reveals that GS15 is mainly
found in the medial-cisternae of the Golgi apparatus and adjacent
tubulo-vesicular elements. Coimmunoprecipitation experiments suggest
that GS15 exists in a distinct SNARE complex that contains SNAREs
(syntaxin5, GS28, and Ykt6) that are implicated in both ER-to-Golgi and
intra-Golgi transport but not with SNAREs involved exclusively in
ER-to-Golgi traffic. Furthermore, components of COPI coat can be
selectively coimmunoprecipitated with GS15 from Golgi extracts.
Overexpression of mutant forms of GS15 affects the normal distribution
of cis- and medial-Golgi proteins (GS28, syntaxin 5, and
Golgi mannosidase II), whereas proteins of the trans-Golgi and TGN
(Vti1-rp2/Vti1a and syntaxin 6) and Golgi matrix/scaffold (GM130 and
p115) are less affected. When the level of GS15 is reduced by duplex
21-nt small interfering RNA (siRNA)-mediated knockdown approach,
diverse markers of the Golgi apparatus are redistributed into small
dotty and diffuse labeling, suggesting an essential role of GS15 in the
Golgi apparatus.
The Institute for
Molecular Bioscience, University of Queensland, St. Lucia, Brisbane,
Qld 4072, Australia; and Diabetes and Metabolism
Research Program, Garvan Institute of Medical Research, St. Vincent's
Hospital, Darlinghurst, NSW 2010, Sydney, Australia
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