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Molecular Chaperones in Signal Transduction

  • Chapter
Molecular Chaperones in Health and Disease

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 172))

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 asphosphorylation, 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 potein kinases. Furthermore, new classes of specific chaperones are emerging and their role in histone-mediated chromatin remodeling and RNA folding are under investigation.

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  1. Institute of Biochemistry, Medical School Hannover, Carl-Neuberg-Str. 1, 30625, Hannover, Germany

    M. Gaestel

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  1. M. Gaestel
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  1. Freiburg i.

    K. Starke

  2. Medical School Hannover, Carl-Neuberg-Str. 1, 30625, Hannover, Germany

    Matthias Gaestel (Professor) (Professor)

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Gaestel, M. (2006). Molecular Chaperones in Signal Transduction. In: Starke, K., Gaestel, M. (eds) Molecular Chaperones in Health and Disease. Handbook of Experimental Pharmacology, vol 172. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-29717-0_4

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