Most S100 proteins are Ca2+-binding proteins involved in Ca2+-signal transduction. They have a well-conserved EF-hand Ca2+-binding motif and a second atypical EF-hand. S100s form stable symmetric homodimers and in the presence of appropriate binding targets, dissociation constants for Ca2+-binding reach physiological levels. S100 proteins are generally constitutively expressed in a cell-specific manner. Several are induced by growth factors, cytokines, or Toll-like receptor (TLR) ligands, in processes associated with stress responses, an activated innate immune system, tumorigenesis, and/or tissue repair. In addition to functions as intracellular regulators, many S100 proteins act extracellularly and particular posttranslational modifications can promote changes in extracellular function. Receptors have been elusive, but include the receptor for advanced glycation end products (RAGE), N-glycans and TLRs.
Several classes of Ca2+-binding proteins have evolved from...
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