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Vol. 13, Issue 1, 119-133, January 2002
Department of Cell Biology, University of
Alberta, Edmonton, Alberta T6G 2H7, Canada
Activation of several ADP-ribosylation factors (ARFs)
by guanine nucleotide exchange factors (GEFs) regulates
recruitment of coat proteins (COPs) on the Golgi complex and
is generally assumed to be the target of brefeldin A (BFA).
The large ARF-GEFs Golgi-specific BFA resistance factor 1 (GBF1) and BFA-inhibited GEFs (BIGs) localize to this
organelle but catalyze exchange preferentially on class II
and class I ARFs, respectively. We now demonstrate using
quantitative confocal microscopy that these GEFs show a very
limited overlap with each other (15 and 23%). In contrast, GBF1 colocalizes with the cis-marker p115
(86%), whereas BIGs overlap extensively with TGN38
(83%). Consistent with these distributions, GBF1, but not
BIG1, partially relocalized to peripheral sites after
incubation at 15°C. The new GBF1 structures represent
peripheral vesicular tubular clusters (VTCs) because 88% of
structures analyzed stained for both GBF1 and p115.
Furthermore, as expected of VTCs, they rapidly reclustered
to the Golgi complex in a microtubule-dependent manner upon
warm-up. These observations suggest that GBF1 and BIGs
activate distinct subclasses of ARFs in specific locations to regulate different types of reactions. In agreement with
this possibility, COPI overlapped to a greater extent with
GBF1 (64%) than BIG1 (31%), whereas clathrin showed
limited overlap with BIG1, and virtually none with GBF1.
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