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Role of Rab9 GTPase in Facilitating Receptor Recruitment by TIP47
Kate S. Carroll,John Hanna,Iris Simon,*Jeff Krise,Pierre Barbero,Suzanne R. Pfeffer
Mannose 6-phosphate receptors (MPRs) deliver lysosomal
hydrolases from the Golgi to endosomes and then return to the Golgicomplex. TIP47 recognizes the cytoplasmic domains of MPRs andis
required for endosome-to-Golgi transport. Here we show thatTIP47 also
bound directly to the Rab9 guanosine triphosphatase(GTPase) in its
active, GTP-bound conformation. Moreover, Rab9increased the affinity
of TIP47 for its cargo. A functional Rab9binding site was required for
TIP47 stimulation of MPR transportin vivo. Thus, a cytosolic cargo
selection device may be selectivelyrecruited onto a specific
organelle, and vesicle budding mightbe coupled to the presence of an
active Rab GTPase.
Department of Biochemistry, Stanford University School of
Medicine, Stanford, CA 94305-5307, USA.
*
Present address: Eos Biotechnology Inc., South San Francisco, CA
94080.
To whom correspondence should be addressed. E-mail:
pfeffer{at}cmgm.stanford.edu
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Nava Segev (18 May 2001) Science292 (5520), 1313.
[DOI: 10.1126/science.1061114] |Summary »|Full Text »
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