4.3 Review

S100A11: Diverse Function and Pathology Corresponding to Different Target Proteins

Journal

CELL BIOCHEMISTRY AND BIOPHYSICS
Volume 55, Issue 3, Pages 117-126

Publisher

HUMANA PRESS INC
DOI: 10.1007/s12013-009-9061-8

Keywords

S100 proteins; S100A11; Cell growth regulation; Cancer development

Funding

  1. National 863 Program of Hi-Tech Research and Development of China [2007AA02Z100]

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S100A11, as a member of S100 protein family, while featuring the common identities as the other EF-hand Ca2+-binding family members, has its own individual characteristics. S100A11 is widely expressed in multiple tissues, and is located in cytoplasm, nucleus, and even cell periphery. S100A11 exists as a non-covalent homodimer with an antiparallel conformation. Ca2+ binding to S100A11 would trigger conformational changes which would expose the hydrophobic cleft of S100A11 and facilitate its interaction with target proteins. Since S100A11 appears to lack enzymatic activity, in this article, corresponding to a variety of its target proteins, we systematically describe the biological roles of S100A11 and its possible mechanism in the processes of inflammation, regulation of enzyme activity, and cell growth regulation. As a dual cell growth mediator, S100A11 acts as either a tumor suppressor or promoter in many different types of tumors and would play respective roles in influencing the proliferation of the cancer cells. We intend to illustrate the biological function of the S100 protein, and shed light on the further research, which will provide us with a better understanding of it.

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