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Description

The Heat Shock Protein 90 family is known as a group of molecular chaperones involved in the regulation of maturation, degradation, and folding transport for a select, yet varied group of proteins primarily comprised of signaling molecules, but also including tyrosine kinases, G-protein subunits, transcription factors, and telomerase. Heat Shock Protein 90 has two isoforms that share a homology of 76%, Heat Shock Protein 90alpha (HSP90alpha) and Heat Shock Protein 90beta (HSP90beta). HSP90alpha contains a charged sequence linker, a C-terminal domain, and N-terminal domain and a middle domain. It is induced by oxidative stress and has been observed in exosomes where it is secreted into the extracellular environment following translocation via TGFalpha stimulus. Extracellular HSP90alpha functions to facilitate the migration of both dermal and epidermal cells through its interaction with cell surface receptors CD91 and LRP1. HSP90alpha interaction with TERT is a necessary component of TERT holoenzyme complex assembly and stabilization. It has also been shown to interact with a variety of other proteins such as FNIP1, HSF1, TOM34, AHSA1, SMYD3, and DNAJC7.