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

Bayer, Michael, Fischer, Julia, Kremerskothen, Joachim, Ossendorf, Edith, Matanis, Theodoros, Konczal, Magdalena, Weide, Thomas, Barnekow, Angelika·2005·BMC Cell Biology
DOI 10.1186/1471-2121-6-15PMC PMC1079803
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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. 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 r ab 1b inding 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.

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  • RUSC2 interacts with the Golgi protein GM130 and has been proposed as a potential regulator of endosomal targeting of vesicles derived from the endoplasmic reticulum.

    “RUSC2 has also been reported to interact with the Golgi protein GM130 and has been proposed as a potential regulator of endosomal targeting of vesicles derived from the endoplasmic reticulum (ER) (50).”

    From EHD1 and RUSC2 Control Basal Epidermal Growth Factor Receptor Cell Surface Expression and Recycling (2020) · cites this paper as [50]

  • RUSC2-interacting small G-protein Rab1a regulates trafficking from the Golgi compartment to the plasma membrane.

    “Given the above results, the reported RUSC2 interaction with GM130 (50) and the role of RUSC2-interacting small G-protein Rab1a in regulating trafficking from the Golgi compartment to the plasma membrane (50, 69, 70), we reasoned that RUSC2 may also function in EHD1-dependent EGFR trafficking out of the Golgi compartment.”

    From EHD1 and RUSC2 Control Basal Epidermal Growth Factor Receptor Cell Surface Expression and Recycling (2020) · cites this paper as [50]

  • RUSC2 directly interacts with GM130 and with Golgi-associated Rab1.

    “Given the previous reports that RUSC2 directly interacts with GM130 as well as with Golgi-associated Rab1 (50), the prominent colocalization of RUSC2 with EHD1 led us to hypothesize that RUSC2, similar to EHD1, may function to promote the EGFR trafficking out of the Golgi compartment.”

    From EHD1 and RUSC2 Control Basal Epidermal Growth Factor Receptor Cell Surface Expression and Recycling (2020) · cites this paper as [50]

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Authors
Bayer, M., Fischer, J., Kremerskothen, J., Ossendorf, E., Matanis, T., Konczal, M., Weide, T., & Barnekow, A.
Venue
BMC Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2005-03-29
Volume
6
Issue
1
ISSN
1471-2121
DOI
10.1186/1471-2121-6-15
PMC
PMC1079803
Cited by
31
References
0
Language
en
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