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sHsp-Phosphorylation: Enzymes, Signaling Pathways and Functional Implications

  • Chapter
Small Stress Proteins

Part of the book series: Progress in Molecular and Subcellular Biology ((PMSB,volume 28))

Abstract

Several posttranslational modifications of sHsps have been detected, including phosphorylation (Kim et al. 1983; Voorter et al. 1986), deamidation, acylation as well as mixed intermolecular disulfide formation, oxidation and glycation (for a review of the latter modifications, see Groenen et al. 1994). In this chapter, one of the most prominent modifications, the sHsp phosphorylation, the enzymes responsible for this modification as well as the possible functional implications will be reviewed in detail. However, it might well be that phosphorylation regulates sHsp structure and function in a complex interplay with some of the other modifications mentioned above.

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  1. M. Gaestel

    Present address: Center Biochemistry/Institute of Biochemistry, Medical School Hannover, Carl-Neuberg-Str. 1, 30625, Hannover, Germany

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  1. Institut für Pharmazeutische Biologie, Martin-Luther-Universität Halle/Wittenberg, Hoher Weg 8, 06120, Halle, Germany

    M. Gaestel

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  1. Laboratoire Stress Oxydant Chaperons et Apoptose Centre de Génétique Moléculaire et Cellulaire CNRS UMR-5534, Université Claude Bernard Lyon-I, 43, Bd. du 11 Novembre, 69622, Villeurbanne, France

    André-Patrick Arrigo

  2. Institut für Physiologische Chemie Abteilung für Angewandte Molekularbiologie, Johannes Gutenberg-Universität, Duesbergweg 6, 55099, Mainz, Germany

    W. E. G. Müller

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Gaestel, M. (2002). sHsp-Phosphorylation: Enzymes, Signaling Pathways and Functional Implications. In: Arrigo, AP., Müller, W.E.G. (eds) Small Stress Proteins. Progress in Molecular and Subcellular Biology, vol 28. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56348-5_8

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  • DOI: https://doi.org/10.1007/978-3-642-56348-5_8

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