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Bestrophin 1

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Bestrophin 1

Bestrophin 1
Symbols  ; ARB; BEST; BMD; RP50; TU15B; VMD2
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Bestrophin-1 is a protein that in humans is encoded by the BEST1 gene.[1][2][3]

It can be associated with Vitelliform macular dystrophy.


BEST1 belongs to the bestrophin family of calcium-activated anion channels, which includes BEST2, BEST3, and BEST4. Bestrophins are transmembrane (TM) proteins that share a homology region containing a high content of aromatic residues, including an invariant arg-phe-pro (RFP) motif. Bestrophins are believed to function as chloride channels that may also serve as regulators of intracellular calcium signalling.[4]

Bestrophin 1 was shown to be permeable for chloride, thiocyanate, bicarbonate, glutamate, and GABA. Bestrophin 1-mediated GABA release has recently been demonstrated to be responsible for tonic inhibition in cerebellar granule cells,[5] and has been linked to the pathology of Alzheimer's disease.[6]

Gene structure

The bestrophin genes share a conserved gene structure, with almost identical sizes of the 8 RFP-TM domain-encoding exons and highly conserved exon-intron boundaries. Each of the 4 bestrophin genes has a unique 3-prime end of variable length.[3][7][8]

BEST1 has been shown by two independent studies to be regulated by Microphthalmia-associated transcription factor.[9][10]


Bestrophin 1 has been shown to interact with PPP2CA.[11][3]



  1. ^ Stone EM, Nichols BE, Streb LM, Kimura AE, Sheffield VC (Jun 1993). "Genetic linkage of vitelliform macular degeneration (Best's disease) to chromosome 11q13". Nat Genet 1 (4): 246–50.  
  2. ^ Barro Soria R, Spitzner M, Schreiber R, Kunzelmann K (Sep 2006). conductance in epithelia" activated Cl2+"Bestrophin 1 enables Ca. J Biol Chem 284 (43): 29405–12.  
  3. ^ a b "Entrez Gene: BEST1 bestrophin 1". 
  4. ^ Hartzell HC, Qu Z, Yu K, Xiao Q, Chien LT (April 2008). "Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies". Physiol. Rev. 88 (2): 639–72.  
  5. ^ Lee S, Yoon BE, Berglund K, Oh SJ, Park H, Shin HS, Augustine GJ, Lee CJ (November 2010). "Channel-mediated tonic GABA release from glia". Science 330 (6005): 790–6.  
  6. ^ Jo, Seonmi (2014). "GABA from reactive astrocytes impairs memory in mouse models of Alzheimer's disease". Nature Medicine 20 (8): 886–896.  
  7. ^ Stöhr H, Marquardt A, Nanda I, Schmid M, Weber BH (April 2002). "Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family". Eur. J. Hum. Genet. 10 (4): 281–4.  
  8. ^ Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J (October 2003). "Structure-function analysis of the bestrophin family of anion channels". J. Biol. Chem. 278 (42): 41114–25.  
  9. ^ Esumi N, Kachi S, Campochiaro PA, Zack DJ (2007). "VMD2 promoter requires two proximal E-box sites for its activity in vivo and is regulated by the MITF-TFE family". J. Biol. Chem. 282 (3): 1838–50.  
  10. ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76.  
  11. ^ Marmorstein LY, McLaughlin PJ, Stanton JB, Yan L, Crabb JW, Marmorstein AD (2002). "Bestrophin interacts physically and functionally with protein phosphatase 2A". J. Biol. Chem. 277 (34): 30591–7.  
  12. ^ 2012; 4(S4):195-200.International Journal of Pharmacy and Pharmaceutical SciencesRao PR. Identification of novel selective antagonists for Bestrophin-1 protein by homology modeling and molecular docking.

Further reading

External links

  • GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview

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