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Molecular Physiology of Bestrophins: Multifunctional Membrane Proteins Linked to Best Disease and Other Retinopathies

Department of Cell Biology, Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia

This article reviews the current state of knowledge about the bestrophins, a newly identified family of proteins that can function both as Cl^– channels and as regulators of voltage-gated Ca²⁺ channels. The founding member, human bestrophin-1 (hBest1), was identified as the gene responsible for a dominantly inherited, juvenile-onset form of macular degeneration called Best vitelliform macular dystrophy. Mutations in hBest1 have also been associated with a small fraction of adult-onset macular dystrophies. It is proposed that dysfunction of bestrophin results in abnormal fluid and ion transport by the retinal pigment epithelium, resulting in a weakened interface between the retinal pigment epithelium and photoreceptors. There is compelling evidence that bestrophins are Cl^– channels, but bestrophins remain enigmatic because it is not clear that the Cl^– channel function can explain Best disease. In addition to functioning as a Cl^– channel, hBest1 also is able to regulate voltage-gated Ca²⁺ channels. Some bestrophins are activated by increases in intracellular Ca²⁺ concentration, but whether bestrophins are the molecular counterpart of Ca²⁺-activated Cl^– channels remains in doubt. Bestrophins are also regulated by cell volume and may be a member of the volume-regulated anion channel family.

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				Z. Qu and H. C. Hartzell Bestrophin Cl- channels are highly permeable to HCO3- Am J Physiol Cell Physiol, June 1, 2008; 294(6): C1371 - C1377. [Abstract] [Full Text] [PDF]

				K. Yu, Q. Xiao, G. Cui, A. Lee, and H. C. Hartzell The Best Disease-Linked Cl- Channel hBest1 Regulates CaV1 (L-type) Ca2+ Channels via src-Homology-Binding Domains J. Neurosci., May 28, 2008; 28(22): 5660 - 5670. [Abstract] [Full Text] [PDF]