Identification of alpha-tubulin as an hsp105alpha-binding protein by the yeast two-hybrid system.
Hsp105alpha is a mammalian stress protein that belongs to the HSP105/110 family. Hsp105alpha prevents stress-induced apoptosis in neuronal cells and binds to Hsp70/Hsc70 and suppresses the Hsp70 chaperone activity in vitro. In this study, to further elucidate the function of Hsp105alpha, we searched for Hsp105alpha-binding proteins by screening a mouse ... FM3A cell cDNA library with full-length Hsp105alpha using the yeast two-hybrid system and obtained alpha-tubulin as an Hsp105alpha-binding protein. Hsp105alpha bound directly to alpha-tubulin both in vitro and in vivo. Indirect immunofluorescence analysis with anti-Hsp105 and anti-alpha-tubulin antibodies indicated that Hsp105alpha was colocalized with microtubules. Furthermore, the disorganization of microtubules induced by heat shock was prevented in Hsp105alpha-overexpressing COS-7 cells. These findings suggested that Hsp105alpha associates with alpha-tubulin and microtubules in cells and plays a role in protection of microtubules under conditions of stress.
Mesh Terms:
Animals, Apoptosis, COS Cells, DNA, Complementary, Eukaryotic Cells, HSP110 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Heat-Shock Response, Hela Cells, Humans, Mice, Microtubules, Protein Binding, Protein Structure, Tertiary, Recovery of Function, Stress, Physiological, Tubulin, Two-Hybrid System Techniques
Animals, Apoptosis, COS Cells, DNA, Complementary, Eukaryotic Cells, HSP110 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Heat-Shock Response, Hela Cells, Humans, Mice, Microtubules, Protein Binding, Protein Structure, Tertiary, Recovery of Function, Stress, Physiological, Tubulin, Two-Hybrid System Techniques
Exp. Cell Res.
Date: Jun. 10, 2003
PubMed ID: 12749852
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