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Vol. 9, Issue 11, 3241-3257, November 1998
and
*Department of Biochemistry, The rab11 GTPase has been localized to both the Golgi and
recycling endosomes; however, its Golgi-associated function has remained obscure. In this study, rab11 function in exocytic transport was analyzed by using two independent means to perturb its activity. First, expression of the dominant interfering rab11S25N mutant protein
led to a significant inhibition of the cell surface transport of
vesicular stomatitis virus (VSV) G protein and caused VSV G protein to
accumulate in the Golgi. On the other hand, the expression of wild-type
rab11 or the activating rab11Q70L mutant had no adverse effect on VSV G
transport. Next, the membrane association of rab11, which is crucial
for its function, was perturbed by modest increases in GDP dissociation
inhibitor (GDI) levels. This led to selective inhibition of the
trans-Golgi network to cell surface delivery, whereas
endoplasmic reticulum-to-Golgi and intra-Golgi transport were largely
unaffected. The transport inhibition was reversed specifically by
coexpression of wild-type rab11 with GDI. Under the same conditions two
other exocytic rab proteins, rab2 and rab8, remained membrane bound,
and the transport steps regulated by these rab proteins were
unaffected. Neither mutant rab11S25N nor GDI overexpression had any
impact on the cell surface delivery of influenza hemagglutinin. These
data show that functional rab11 is critical for the export of a
basolateral marker but not an apical marker from the trans-Golgi
network and pinpoint rab11 as a sensitive target for inhibition by
excess GDI.
#
Corresponding Author: Department of Pathology,
2325 Camino de Salud, Room 225, University of New Mexico Health
Sciences Center, Albuquerque, NM 87131. E-mail address: wness{at}unm.edu.
Present address: Department of Pathology,
University of New Mexico Health Sciences Center, Albuquerque, NM 87131.
Present address: Harvard Institute of Chemistry
and Cell Biology, Harvard Medical School, Boston, MA 02115.
Present address: Laboratory of Infectious
Diseases, National Institute of Allergic and Infectious Diseases,
National Institutes of Health, 7 Center Drive, Bethesda, MD
20892-0720.
Molecular Biology of the Cell
Vol. 9, 3241-3257, November 1998
Copyright © 1998 by The American Society for Cell Biology
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 C. Dumanchin, C. Czech, D. Campion, M. H. Cuif, T. Poyot, C. Martin, F. Charbonnier, B. Goud, L. Pradier, and T. Frebourg Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport Hum. Mol. Genet., July 1, 1999; 8(7): 1263 - 1269. [Abstract] [Full Text] [PDF]
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P. Luan, W. E. Balch, S. D. Emr, and C. G. Burd Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo. Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS J. Biol. Chem., May 21, 1999; 274(21): 14806 - 14817. [Abstract] [Full Text] [PDF]
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J. Zeng, M. Ren, D. Gravotta, C. De Lemos-Chiarandini, M. Lui, H. Erdjument-Bromage, P. Tempst, G. Xu, T. H. Shen, T. Morimoto, et al. Identification of a putative effector protein for rab11 that participates in transferrin recycling PNAS, March 16, 1999; 96(6): 2840 - 2845. [Abstract] [Full Text] [PDF]
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M Trischler, W Stoorvogel, and O Ullrich Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway J. Cell Sci., January 12, 1999; 112(24): 4773 - 4783. [Abstract] [PDF]
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A. Mammoto, T. Sasaki, Y. Kim, and Y. Takai Physical and Functional Interaction of Rabphilin-11 with Mammalian Sec13 Protein. IMPLICATION IN VESICLE TRAFFICKING J. Biol. Chem., April 28, 2000; 275(18): 13167 - 13170. [Abstract] [Full Text] [PDF]
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R. Shirakawa, A. Yoshioka, H. Horiuchi, H. Nishioka, A. Tabuchi, and T. Kita Small GTPase Rab4 Regulates Ca2+-induced alpha -Granule Secretion in Platelets J. Biol. Chem., October 20, 2000; 275(43): 33844 - 33849. [Abstract] [Full Text] [PDF]
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