Identification and characterization of Iporin as a novel interaction partner for rab1
| Autor: | Michael, Bayer, Julia, Fischer, Joachim, Kremerskothen, Edith, Ossendorf, Theodoros, Matanis, Magdalena, Konczal, Thomas, Weide, Angelika, Barnekow |
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| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Base Sequence
lcsh:Cytology Molecular Sequence Data Mutation Missense Membrane Proteins Biological Transport Endoplasmic Reticulum Autoantigens rab1 GTP-Binding Proteins src Homology Domains Cytosol Two-Hybrid System Techniques Humans Tissue Distribution lcsh:QH573-671 Carrier Proteins Peptides Protein Binding Research Article |
| Zdroj: | BMC Cell Biology, Vol 6, Iss 1, p 15 (2005) BMC Cell Biology |
| ISSN: | 1471-2121 |
| Popis: | 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-interacting protein. It was initially identified by yeast two-hybrid screening experiments with the active mutant of rab1b (rab1b Q67R) as bait. Iporin contains a SH3 domain and two polyproline stretches, which are known to play a role in protein/protein interactions. In addition, Iporin encloses a RUN domain, which seems to be a major part of the rab1binding domain (R1BD). Iporin is ubiquitously expressed and immunofluorescence staining displays a cytosolic punctual distribution. Interestingly, we also show that Iporin interacts with another rab1 interacting partner, the GM130 protein. Conclusion Our results demonstrate that Iporin is a potential new interacting partner of rab1. Iporin is different from already identified rab1 interacting proteins concerning protein structure and cellular localization. We conclude that Iporin might function as a link between the targeting of ER derived vesicles, triggered by the rab1 GTPase and a signaling pathway regulated by molecules containing SH3 and/or poly-proline regions. The characterization of this novel intermolecular relation could help to elucidate how vesicles find their way from ER to the Golgi apparatus. |
| Databáze: | OpenAIRE |
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