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J Biol Chem, Vol. 274, Issue 36, 25517-25524, September 3, 1999
From the Department of Molecular Biology and Biochemistry, Osaka
University Medical School, Suita 565-0871, Japan
Rab11 small G protein has been implicated in
vesicle recycling, but its upstream regulators or downstream targets
have not yet been identified. We isolated here a downstream target of
Rab11, named rabphilin-11, from bovine brain. Moreover, we isolated
from a rat brain cDNA library its cDNA, which encoded a protein
with a Mr of 100,946 and 908 amino acids (aa).
Rabphilin-11 bound GTP-Rab11 more preferentially than GDP-Rab11 at the
N-terminal region and was specific for Rab11 and inactive for other Rab
and Rho small G proteins. Both GTP-Rab11 and rabphilin-11 were
colocalized at perinuclear regions, presumably the Golgi complex and
recycling endosomes, in Madin-Darby canine kidney cells. In HeLa cells
cultured on fibronectin, both the proteins were localized not only at
perinuclear regions but also along microtubules, which were oriented
toward membrane lamellipodia. Treatment of HeLa cells with nocodazole caused disruption of microtubules and dispersion of GTP-Rab11 and
rabphilin-11. Overexpression of the C-terminal fragment of rabphilin-11
(aa 607-730), lacking the GTP-Rab11 binding domain, in HeLa cells
reduced accumulation of transferrin at perinuclear regions and cell
migration. Rabphilin-11 turned out to be a rat counterpart of recently
reported bovine Rab11BP. These results indicate that rabphilin-11 is a
downstream target of Rab11 which is involved in vesicle recycling.
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