A truncated form of α-tubulin detected in purified proteasome complexes
- Autores: Ivanova E.1,2, Artamonova T.3, Zaikova Y.2, Khodorkovskii M.3, Tsimokha A.2
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Afiliações:
- St. Petersburg State University
- Institute of Cytology
- Nanobiotechnogy Center
- Edição: Volume 11, Nº 3 (2017)
- Páginas: 191-196
- Seção: Article
- URL: https://journals.rcsi.science/1990-519X/article/view/212347
- DOI: https://doi.org/10.1134/S1990519X1703004X
- ID: 212347
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Resumo
The 26S proteasome is a multisubunit protein complex responsible for selective protein degradation in the cell. A number of proteins with known and unknown functions were shown to be permanently or temporarily associated with 26S proteasomes. Identification of proteins that interact with proteasomes is an important step in the understanding of the proteasome functions in the cell and the mechanisms of their regulation. Using MALDI–ICR mass spectrometry, we have shown that some proteins of the cytoskeleton, such as actin, α-actinin 4, and α- and β-tubulins are associated with proteasomes obtained by affinity purification from the human myelogenous leukemia cell line K562. Western blot analysis showed that a truncated form of α-tubulin was associated with the purified proteasomes. The presence of the α-tubulin isoform in complex with affinity purified proteasomes was also observed in the human embryonic kidney cell line 293.
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Sobre autores
E. Ivanova
St. Petersburg State University; Institute of Cytology
Autor responsável pela correspondência
Email: ivanoval.027@gmail.com
Rússia, St. Petersburg, 199034; St. Petersburg, 194064
T. Artamonova
Nanobiotechnogy Center
Email: atsimokha@incras.ru
Rússia, St. Petersburg, 195251
Yu. Zaikova
Institute of Cytology
Email: atsimokha@incras.ru
Rússia, St. Petersburg, 194064
M. Khodorkovskii
Nanobiotechnogy Center
Email: atsimokha@incras.ru
Rússia, St. Petersburg, 195251
A. Tsimokha
Institute of Cytology
Autor responsável pela correspondência
Email: atsimokha@incras.ru
Rússia, St. Petersburg, 194064