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Gene Review:

S100B - S100 calcium binding protein B

Gallus gallus

Arcuri, C. et al., Arcuri, C. et al., Wear, M.A. et al.

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High impact information on S100B

Capping protein binding to S100B: implications for the tentacle model for capping the actin filament barbed end [1].
In the NMR structure of S100B complexed with the alpha-subunit-derived 12-amino acid peptide, the hydrophobic side of a short alpha-helix in the peptide, containing an important tryptophan residue, contacts S100B [1].
Immunoprecipitation studies indicated that ANXA6/S100A1 and ANXA6/S100B complexes formed in vivo [2].
At E15, S100A11 was found on the sarcolemma and internal membranes, likely longitudinal tubules, where the protein was co-localized in part with S100A1 and S100B [3].
Analyses of alpha-actinin, S100A1 and S100B were done in parallel for comparison [3].

Anatomical context of S100B

Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles [2].
These four proteins displayed distinct expression patterns, ANXA5 being the first to be expressed in myotubes (i.e. at embryonic day 8), followed by ANXA6 (at embryonic day 12) and S100A1 and S100B (between embryonic day 12 and embryonic day 15) [2].

Associations of S100B with chemical compounds

Our data suggests that, like S100A1 and S100B, S100A11 might have a role in the regulation of membrane activities, probably in relation to Ca(2+) fluxes in skeletal muscle cells [3].

References

Capping protein binding to S100B: implications for the tentacle model for capping the actin filament barbed end. Wear, M.A., Cooper, J.A. J. Biol. Chem. (2004) [Pubmed]
Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles. Arcuri, C., Giambanco, I., Bianchi, R., Donato, R. Neuroscience (2002) [Pubmed]
Subcellular localization of S100A11 (S100C, calgizzarin) in developing and adult avian skeletal muscles. Arcuri, C., Giambanco, I., Bianchi, R., Donato, R. Biochim. Biophys. Acta (2002) [Pubmed]

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