Article ID Journal Published Year Pages File Type
7633562 Journal of Proteomics 2018 24 Pages PDF
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 ΔN-HtrA3L/S proteins. They cleave efficiently vimentin and β-tubulin, and less efficiently- actin; they also stimulate tubulin polymerization. The ΔN-HtrA3S is more active than the ΔN-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
Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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