title: Molecular chaperones in signal transduction.
abstract: Many cellular signaling molecules exist in different conformations corresponding to active and inactive states. Transition between these states is regulated by reversible modifications, such as phosphorylation, or by binding of nucleotide triphosphates, their regulated hydrolysis to diphosphates, and their exchange against fresh triphosphates. Specificity and efficiency of cellular signaling is further maintained by regulated subcellular localization of signaling molecules as well as regulated protein-protein interaction. Hence, it is not surprising that molecular chaperones--proteins that are able to specifically interact with distinct conformations of other proteins--could per se interfere with cellular signaling. Hence, it is not surprising that chaperones have co-evolved as integral components of signaling networks where they can function in the maturation as well as in regulating the transition between active and inactive state of signaling molecules, such as receptors, transcriptional regulators and protein kinases. Furthermore, new classes of specific chaperones are emerging and their role in histone-mediated chromatin remodeling and RNA folding are under investigation.
authors.affiliation: Institute of Biochemistry, Medical School Hannover, Germany. gaestel.matthias@mh-hannover.de
authors.forename: M
authors.initials: M
authors.lastname: Gaestel
mesh_terms: D000818:Animals; D004268:DNA-Binding Proteins / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D018841:HSP90 Heat-Shock Proteins / Q000502:physiology; D000076249:Heat Shock Transcription Factors; D006657:Histones / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D017510:Protein Folding; D011494:Protein Kinases / Q000502:physiology; D012313:RNA / Q000502:physiology; D018160:Receptors, Cytoplasmic and Nuclear / Q000502:physiology; D017978:Receptors, Growth Factor / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology; D048051:p38 Mitogen-Activated Protein Kinases / Q000502:physiology
chemical_list: D004268:DNA-Binding Proteins; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D000076249:Heat Shock Transcription Factors; D006657:Histones; D018832:Molecular Chaperones; D018160:Receptors, Cytoplasmic and Nuclear; D017978:Receptors, Growth Factor; D014157:Transcription Factors; D012313:RNA; D011494:Protein Kinases; D048051:p38 Mitogen-Activated Protein Kinases