title: Hsp90--from signal transduction to cell transformation.
abstract: The molecular chaperone, Hsp90, facilitates the maturation and/or activation of over 100 'client proteins' involved in signal transduction and transcriptional regulation. Largely an enigma among the families of heat shock proteins, Hsp90 is central to processes broadly ranging from cell cycle regulation to cellular transformation. Here, we review the contemporary body of knowledge regarding the biochemical mechanisms of Hsp90 and update the most current paradigms defining its involvement in both normal and pathological cell physiology.
authors.affiliation: Section of Molecular Genetics and Microbiology and Institute for Cellular and Molecular Biology, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Brown
authors.forename: Li
authors.initials: L
authors.lastname: Zhu
authors.forename: Christian
authors.initials: C
authors.lastname: Schmidt
authors.forename: Philip W
authors.initials: PW
authors.lastname: Tucker
mesh_terms: D000818:Animals; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000502:physiology*; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D015398:Signal Transduction / Q000502:physiology*; D015533:Transcriptional Activation / Q000502:physiology*