Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7633562 | Journal of Proteomics | 2018 | 24 Pages |
Abstract
Model of the HtrA3 interactions with cytoskeleton proteins and TCP1α chaperonin. Translocation of HtrA3 from mitochondria is accompanied by removal of the N-terminal Mac25 domain [19], resulting in formation of the ÎN-HtrA3L/S proteins. They cleave efficiently vimentin and β-tubulin, and less efficiently- actin; they also stimulate tubulin polymerization. The ÎN-HtrA3S is more active than the ÎN-HtrA3L in the degradation but less active in the polymerization. HtrA3 may act as a co-chaperone, possibly in cooperation with TCP1α, in tubulin polymerization. The HtrA3 influence on the cytoskeleton dynamics may be one of the ways in which this protease/chaperone promotes cell death.77
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Tomasz Wenta, Dorota Zurawa-Janicka, Michal Rychlowski, Miroslaw Jarzab, Przemyslaw Glaza, Andrea Lipinska, Krystyna Bienkowska-Szewczyk, Anna Herman-Antosiewicz, Joanna Skorko-Glonek, Barbara Lipinska,