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Vol. 11, Issue 2, 635-645, February 2000
and
*Cell Biology Laboratory, Imperial Cancer Research Fund, London
WC2A 3PX, United Kingdom; and §Department of Cell
Biology, Yale University School of Medicine, New Haven, Connecticut
06520-8002
Biochemical data have shown that COPI-coated vesicles are tethered
to Golgi membranes by a complex of at least three proteins: p115,
giantin, and GM130. p115 binds to giantin on the vesicles and to
GM130 on the membrane. We now examine the function of this tethering
complex in vivo. Microinjection of an N-terminal peptide of GM130 or
overexpression of GM130 lacking this N-terminal peptide inhibits the
binding of p115 to Golgi membranes. Electron microscopic analysis of
single microinjected cells shows that the number of COP-sized transport
vesicles in the Golgi region increases substantially, suggesting that
transport vesicles continue to bud but are less able to fuse. This was
corroborated by quantitative immunofluorescence analysis, which showed
that the intracellular transport of the VSV-G protein was significantly
inhibited. Together, these data suggest that this tethering complex
increases the efficiency with which transport vesicles fuse with their
target membrane. They also provide support for a model of mitotic Golgi
fragmentation in which the tethering complex is disrupted by mitotic
phosphorylation of GM130.
Present address: Institute of
Biotechnology, Electron Microscopy Unit, University of Helsinki,
Viikinkaari 9, 00014 Helsinki, Finland.
Corresponding author. E-mail address:
joachim.seemann{at}yale.edu.
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