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| Content Provider | Springer Nature Link |
|---|---|
| Author | Bobkov, D. E. Aizenshtadt, A. A. Kropacheva, I. V. Pinaev, G. P. |
| Copyright Year | 2012 |
| Abstract | The presence of an actin-binding protein, tropomyosin, in particles or protein complexes not bound with actin structures were found during an assay of structural rearrangements of actin cytoskeleton. To study the composition and properties of these protein complexes, a novel method of their isolation without destroying cytoskeleton structures has been elaborated. The protein composition of isolated tropomyosin particles was assessed by gel filtration, electrophoresis, and Western blotting. It was demonstrated that they are about 700-kDa multimolecular complexes. In addition to tropomyosin and actin, these complexes contained Hsp70, Hsp90, and myosin-9 identified by mass spectrometry. It was found that the deacetylase inhibitor, trichostatin A, which induced actin cytoskeleton rearrangements, changed the number of tropomyosin particles and caused redistribution of tropomyosin between cytosol and cytoskeleton. These results demonstrate that these multimolecular complexes may participate in the process of reorganization of actin microfilaments. |
| Starting Page | 137 |
| Ending Page | 146 |
| Page Count | 10 |
| File Format | |
| ISSN | 1990519X |
| Journal | Cell and Tissue Biology |
| Volume Number | 6 |
| Issue Number | 2 |
| e-ISSN | 19905203 |
| Language | English |
| Publisher | SP MAIK Nauka/Interperiodica |
| Publisher Date | 2012-04-24 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | tropomyosin protein complexes actin cytoskeleton myosin-9 heat shock proteins Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology |
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