Identification and characterization of Iporin as a novel interaction partner for rab1.

ABSTRACT:

Background

The small GTPase rab1a and its isoform rab1b are essential regulating components in the vesicle transport between the ER and the Golgi apparatus. Rab1 is thought to act as a molecular switch and can change between an active GTP-bound and an inactive GDP-bound conformation. To elucidate the function of rab1, several approaches have been established to isolate effector proteins, which interact with the activated conformation of rab1. To date p115, GM130, golgin-84 and MICAL have been identified as direct interacting partners. Together with rab1, these molecules are components of a protein complex, which mediates and regulates intracellular vesicle transport.

Results

Here, we report the characterization of Iporin, which is similar to KIAA0375 as a novel rab1-interact

SUBMITTER: Bayer M 

PROVIDER: S-EPMC1079803 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature