Rab proteins are small GTPases involved in the regulation of intracellular membrane traffic in mammalian cells. In order to find Rab-interacting proteins we performed a two-hybrid screening using a human brain cDNA library. Here we report the isolation of a full-length human cDNA clone coding for a protein of 185 amino acids. This protein interacts strongly with the Rab4b, Rab5a, and Rab5c proteins and weakly with Rab4a, Rab6, Rab7, Rab17, and Rab22 in the two-hybrid assay. Comparison with the Data Bank revealed that this clone represents the human homolog of the previously isolated rat Prenylated Rab Acceptor (rPRA1). Analysis of mRNA expression shows a single abundant mRNA of about 0.8 kb ubiquitously expressed. Western blot analysis of the overexpressed protein shows a band of the expected size equally distributed between cytosol and membranes.

Interaction cloning and characterization of the cDNA encoding the Human Prenylated Rab Acceptor.

BUCCI, Cecilia;
1999-01-01

Abstract

Rab proteins are small GTPases involved in the regulation of intracellular membrane traffic in mammalian cells. In order to find Rab-interacting proteins we performed a two-hybrid screening using a human brain cDNA library. Here we report the isolation of a full-length human cDNA clone coding for a protein of 185 amino acids. This protein interacts strongly with the Rab4b, Rab5a, and Rab5c proteins and weakly with Rab4a, Rab6, Rab7, Rab17, and Rab22 in the two-hybrid assay. Comparison with the Data Bank revealed that this clone represents the human homolog of the previously isolated rat Prenylated Rab Acceptor (rPRA1). Analysis of mRNA expression shows a single abundant mRNA of about 0.8 kb ubiquitously expressed. Western blot analysis of the overexpressed protein shows a band of the expected size equally distributed between cytosol and membranes.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11587/101666
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