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Role of Rab9 GTPase in Facilitating Receptor Recruitment by TIP47

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Science  18 May 2001:
Vol. 292, Issue 5520, pp. 1373-1376
DOI: 10.1126/science.1056791

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Abstract

Mannose 6-phosphate receptors (MPRs) deliver lysosomal hydrolases from the Golgi to endosomes and then return to the Golgi complex. TIP47 recognizes the cytoplasmic domains of MPRs and is required for endosome-to-Golgi transport. Here we show that TIP47 also bound directly to the Rab9 guanosine triphosphatase (GTPase) in its active, GTP-bound conformation. Moreover, Rab9 increased the affinity of TIP47 for its cargo. A functional Rab9 binding site was required for TIP47 stimulation of MPR transport in vivo. Thus, a cytosolic cargo selection device may be selectively recruited onto a specific organelle, and vesicle budding might be coupled to the presence of an active Rab GTPase.

  • * Present address: Eos Biotechnology Inc., South San Francisco, CA 94080.

  • To whom correspondence should be addressed. E-mail: pfeffer{at}cmgm.stanford.edu

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