MAP Kinase Signaling

Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small heat shock proteins, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the expression level of HSP27 increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78 and Ser82 by MAPKAP kinase 2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

1. Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373.
2. Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.
3. Rouse, J. et al. (1994) Cell 78, 1027-1037.
4. Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956.
5. Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214.
6. Rousseau, S. et al. (1997) Oncogene 15, 2169-2177.

• Sarkar, D. et al. (2002) mda-7 (IL-24) mediates selective apoptosis in human melanoma cells by inducing the coordinated overexpression of the GADD family of genes by means of p38 MAPK. Proc. Natl. Acad. Sci. USA 99, 10054-10059. Applications: Western Blotting
• Kennett, S. B. et al. (2004) Requirement of protein kinase C micro activation and calpain-mediated proteolysis for arachidonic acid-stimulated adhesion of MDA-MB-435 human mammary carcinoma cells to collagen type IV. J. Biol. Chem. 279, 3300-3307. Applications: Western Blotting

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HSP27 (G31) Mouse mAb

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