EF-hand Ca2+-binding protein family members, α- and β-parvalbumins have been studied for decades. Yet, considerable information is lacking distinguishing functional differences between mammalian α-parvalbumin (PVALB) and oncomodulin (OCM), a branded β-parvalbumin. Herein, we provide an overview detailing the current body of work centered around OCM as an EF-Hand Ca2+-binding protein and describe potential mechanisms of OCM function within the inner ear and immune cells. Additionally, we posit that OCM is evolutionarily distinct from PVALB and most other β-parvalbumins. This review summarizes recent studies pertaining to the function of OCM and emphasizes OCM as a parvalbumin possessing a unique cell and tissue distribution, Ca2+ buffering capacity and phylogenetic origin.
CITATION STYLE
Climer, L. K., Cox, A. M., Reynolds, T. J., & Simmons, D. D. (2019). Oncomodulin: The Enigmatic Parvalbumin Protein. Frontiers in Molecular Neuroscience, 12. https://doi.org/10.3389/fnmol.2019.00235
Mendeley helps you to discover research relevant for your work.