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Vol. 14, Issue 5, 2116-2127, May 2003
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* Department of Cell Biology, University of Alabama at Birmingham, Birmingham,
Alabama 35924;
Departamento de Bioquímica Clínica, Facultad de Ciencias
Químicas, Universidad Nacional de Córdoba, Argentina
Submitted September 30, 2002;
Revised November 28, 2002;
Accepted January 23, 2003
Monitoring Editor: Jennifer Lippincott-Schwartz
The small GTPase Rab1b is essential for endoplasmic reticulum (ER) to Golgi
transport, but its exact function remains unclear. We have examined the
effects of wild-type and three mutant forms of Rab1b in vivo. We show that the
inactive form of Rab1b (the N121I mutant with impaired guanine nucleotide
binding) blocks forward transport of cargo and induces Golgi disruption. The
phenotype is analogous to that induced by brefeldin A (BFA): it causes
resident Golgi proteins to relocate to the ER and induces redistribution of
ER-Golgi intermediate compartment proteins to punctate structures. The COPII
exit machinery seems to be functional in cells expressing the N121I mutant,
but COPI is compromised, as shown by the release of 
-COP into the
cytosol. Our results suggest that Rab1b function influences COPI recruitment.
In support of this, we show that the disruptive effects of N121I can be
reversed by expressing known mediators of COPI recruitment, the GTPase ARF1
and its guanine nucleotide exchange factor GBF1. Further evidence is provided
by the finding that cells expressing the active form of Rab1b (the Q67L mutant
with impaired GTPase activity) are resistant to BFA. Our data suggest a novel
role for Rab1b in ARF1- and GBF1-mediated COPI recruitment pathway.
Abbreviations used: ER, endoplasmic reticulum; VTC, vesicular tubular clusters; BFA, brefeldin A; GFP, green fluorescent protein, GDI, GDP-dissociation inhibitor; ERGIC, ER-Golgi intermediate compartment; VSV-G, vesicular stomatitis virus glycoprotein.
Corresponding author. E-mail:
esztul{at}uab.edu.
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