S100 proteins are low-molecular-weight calcium-binding proteins of the EF-hand superfamily and appear to be involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation (1). The Calpactin I light chain (S100 calcium-binding protein A10; S100A10) is a member of the S100 family and it forms a heterotetrameric complex with another calcium-binding protein, annexin II(2). S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane (3). The basic unit for S100A10 is a tight, non-covalent dimmer (4). S100A10, as well as a few other members of the S100 family, are suggested as transglutaminase substrates. Also, S100 proteins have been reported to localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events (3).
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