Role of Rab9 GTPase in facilitating receptor recruitment by TIP47 |
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Authors: | Carroll K S Hanna J Simon I Krise J Barbero P Pfeffer S R |
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Affiliation: | Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. |
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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. |
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