Proximity Ligation Analysis of protein-protein interactions between HSP90AB1 and FLNA. HeLa cells were stained with anti-HSP90AB1 rabbit purified polyclonal 1:1200 and anti-FLNA mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1 (MIM 140571), an inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM
OTTHUMP00000016517,OTTHUMP00000016518,OTTHUMP00000016519,OTTHUMP00000039869,heat shock 90kD protein 1, beta,heat shock 90kDa protein 1, beta,heat shock protein beta