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Vol. 11, Issue 11, 3819-3833, November 2000
and
Analysis of the human Rab6A gene structure reveals
the presence of a duplicated exon, and incorporation of either of the
two exons by alternative splicing is shown to generate two Rab6
isoforms named Rab6A and Rab6A', which differ in only three amino acid residues located in regions flanking the PM3 GTP-binding domain of the
proteins. These isoforms are ubiquitously expressed at similar levels,
exhibit the same GTP-binding properties, and are localized to the Golgi
apparatus. Overexpression of the GTP-bound mutants of Rab6A (Rab6A
Q72L) or Rab6A' (Rab6A' Q72L) inhibits secretion in HeLa cells, but
overexpression of Rab6A' Q72L does not induce the redistribution of
Golgi proteins into the endoplasmic reticulum. This suggests that
Rab6A' is not able to stimulate Golgi-to-endoplasmic reticulum
retrograde transport, as described previously for Rab6A. In addition,
Rab6A' interacts with two Rab6A partners, GAPCenA and "clone 1,"
but not with the kinesin-like protein Rabkinesin-6, a Golgi-associated
Rab6A effector. Interestingly, we found that the functional differences
between Rab6A and Rab6A' are contingent on one amino acid (T or A at
position 87). Therefore, limited amino acid substitutions within a Rab
protein introduced by alternative splicing could represent a mechanism
to generate functionally different isoforms that interact with distinct
sets of effectors.
Unité Mixte de Recherche Centre National de la
Recherche Scientifique 144, Institut Curie, 75248 Paris Cedex 05, France; Department of Cell Biology, Institute of
Cellular Signaling, University of Nijmegen, 6500 HB, Nijmegen, The
Netherlands; and §Department of Blood Coagulation, Central
Laboratory of the Netherlands Red Cross Blood Transfusion
Service, 1066 CX, Amsterdam, The Netherlands
Corresponding author. E-mail address:
j.fransen{at}celbi.kun.nl.
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