Identification and characterization of Iporin as a novel interaction partner for rab1 |
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| Authors: | Michael?Bayer Julia?Fischer Joachim?Kremerskothen Edith?Ossendorf Theodoros?Matanis Magdalena?Konczal Thomas?Weide Email author" target="_blank">Angelika?BarnekowEmail author |
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| Institution: | (1) UKM Muenster, Albert-Schweitzer-Str. 33, D-48149 Muenster, Germany;(2) Department of Experimental Tumorbiology, University of Muenster, Badestr. 9, D-48149 Muenster, Germany;(3) Cilian AG, Johann-Krane-Weg 42, D-48149 Muenster, Germany |
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| 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. |
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