T1P47 is a key effector for Rab9 localization

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 hyper-variable domains were generated, and their ability to bind seven Rab effectors was quantified. Two ch...

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Bibliographic Details
Published inThe Journal of cell biology Vol. 173; no. 6; p. 917
Main Authors Aivazian, Dikran, Serrano, Ramon L, Pfeffer, Suzanne
Format Journal Article
LanguageEnglish
Published New York Rockefeller University Press 19.06.2006
Subjects
Cellular biology
Genomics
Membranes
Proteins
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Summary: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 hyper-variable 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. [PUBLICATION ABSTRACT]
ISSN:0021-9525
1540-8140