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Published online 12 June 2006. doi:10.1083/jcb.200510010
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 6, 917-926
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Article

TIP47 is a key effector for Rab9 localization



Dikran Aivazian, Ramon L. Serrano, and Suzanne Pfeffer

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305

Correspondence to Suzanne Pfeffer: pfeffer{at}stanford.edu

The human genome encodes ~70 Rab GTPases that localize to the surfaces of distinct membrane compartments. To investigate the mechanism of Rab localization, chimeras containing heterologous Rab hypervariable domains were generated, and their ability to bind seven Rab effectors was quantified. Two chimeras could bind effectors for two distinctly localized Rabs; a Rab5/9 hybrid bound both Rab5 and Rab9 effectors, and a Rab1/9 hybrid bound to certain Rab1 and Rab9 effectors. These unusual chimeras permitted a test of the importance of effector binding for Rab localization. In both cases, changing the cellular concentration of a key Rab9 effector, which is called tail-interacting protein of 47 kD, moved a fraction of the proteins from their parental Rab localization to that of Rab9. Thus, relative concentrations of certain competing effectors could determine a chimera's localization. These data confirm the importance of effector interactions for Rab9 localization, and support a model in which effector proteins rely on Rabs as much as Rabs rely on effectors to achieve their correct steady state localizations.

Abbreviations used in this paper: CCD, charge-coupled device; CI, cation-independent; EEA, early endosome antigen; GDF, GDI displacement factor; GDI, GDP dissociation inhibitor; GEF, guanine nucleotide exchange factor; MPR, mannose 6-phosphate receptor; TIP47, tail-interacting protein of 47 kD.


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