In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. HSBP1 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores, and high levels are associated with carcinoma of the breast and with endometrial adenocarcinomas. Heat shock of HeLa cell cultures, or treatment with arsenite, phorbol ester, or tumor necrosis factor, causes a rapid phosphorylation of preexisting HSBP1, with Ser82 as the major site and Ser78 the minor site of phosphorylation. HSBP1 may exert phosphorylation-activated functions linked with growth signaling pathways in unstressed cells. A homeostatic function at this level could protect cells from adverse effects of signal transduction systems which may be activated inappropriately during stress.1) Wano, C., et al., Exp. Cell Res. 298(2):584-592 (2004).
							
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