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Dimerization properties of Rabaptin-5 and its isoforms

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Abstract

Rabaptin-5 plays an important role in intracellular membrane traffic acting as an effector molecule of small GTPases Rab5 and Rab4. It was previously demonstrated that Rabaptin-5 exists as a part of a large protein complex in vivo and is able to form dimers in vitro. Data of X-ray structural analysis suggest that dimerization of Rabaptin-5 is an important feature required for its interaction with Rab5 GTPase. Recently several isoforms of Rabaptin-5 characterized by various deletions in the polypeptide chains have been identified. These isoforms might exhibit functional properties that differ from those of Rabaptin-5. In this study, we have investigated dimerization properties of δ and γ isoforms of Rabaptin-5. In addition, we have provided the first direct evidence for Rabaptin-5 dimerization in cells.

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Abbreviations

GAL4BD:

DNA-binding domain of the transcription factor GAL4

GAL4AD:

activation domain of the transcription factor GAL4

Rab5-GTP:

GTP-bound form of Rab5

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Authors and Affiliations

  1. Institute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, 119334, Moscow, Russia

    E. V. Korobko, S. L. Kiselev & I. V. Korobko

  2. Centre for Medical Studies in Russia, University of Oslo, ul. Vavilova 34/5, 119334, Moscow, Russia

    E. V. Korobko

Authors
  1. E. V. Korobko
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  2. S. L. Kiselev
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  3. I. V. Korobko
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Correspondence to I. V. Korobko.

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Original Russian Text © E. V. Korobko, S. L. Kiselev, I. V. Korobko, 2006, published in Biokhimiya, 2006, Vol. 71, No. 12, pp. 1607–1612.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM06-114, September 10, 2006.

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Korobko, E.V., Kiselev, S.L. & Korobko, I.V. Dimerization properties of Rabaptin-5 and its isoforms. Biochemistry (Moscow) 71, 1307–1311 (2006). https://doi.org/10.1134/S0006297906120030

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  • DOI: https://doi.org/10.1134/S0006297906120030

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