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Hsp27 Phosphorylation Patterns and Cellular Consequences

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Cellular Trafficking of Cell Stress Proteins in Health and Disease

Part of the book series: Heat Shock Proteins ((HESP,volume 6))

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Abstract

The human small heat shock protein 27 (HSP27 or HSPB1) is a multifunctional protein that participates in a variety of cellular processes such as controlling protein folding, F-actin-dependent processes, cytoprotection/anti-apoptosis, differentiation, cell proliferation, and gene expression. The structural and physiological properties of HSP27 are partially controlled by phosphorylation and several protein kinases that mediate phosphorylation have been identified. While phosphorylation of serine residues 15, 78 and 82 has been most extensively studied, other in vivo phosphorylation modifications have been identified. Here we review the different phosphorylations of HSP27 and consider the consequences of phosphorylation on HSP27’s conformation, subcellular localization, and cellular roles. We also address the phosphorylation pattern under pathogenic conditions and discuss the possible implications of HSP27 phosphorylation in human disease.

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  1. Institute of Medical Biology, Faculty of Health Sciences, University of Tromsø, NO-9037, Tromsø, Norway

    Ugo Moens & Sergiy Kostenko

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  1. Eastman Dental Institute, Div. Microbial Diseases, University College, London, Gray's Inn Road 256, London, WC1X 8LD, United Kingdom

    Brian Henderson

  2. School of Medicine & Biomedical Science, University of Sheffield, Beech Hill Road, Sheffield, S10 2RX, United Kingdom

    A. Graham Pockley

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Moens, U., Kostenko, S. (2012). Hsp27 Phosphorylation Patterns and Cellular Consequences. In: Henderson, B., Pockley, A. (eds) Cellular Trafficking of Cell Stress Proteins in Health and Disease. Heat Shock Proteins, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4740-1_4

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