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Bestrophin 4

VMD2L2, bestrophin-4
This gene is a member of the bestrophin gene family of anion channels. Bestrophin genes share a similar gene structure with highly conserved exon-intron boundaries, but with distinct 3' ends. Bestrophins are transmembrane proteins that contain a homologous region rich in aromatic residues, including an invariant arg-phe-pro motif. Mutation in one of the family members (bestrophin 1) is associated with vitelliform macular dystrophy. The bestrophin 4 gene is predominantly expressed in the colon. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Best2, VMD2L3, ARB, RFP, ACID
Papers on VMD2L2
Lineage-specific expression of bestrophin-2 and bestrophin-4 in human intestinal epithelial cells.
Watanabe et al., Tokyo, Japan. In Plos One, 2012
Studies have suggested that, among the four human bestrophin-family genes, bestrophin-2 (BEST2) and bestrophin-4 (BEST4) might be expressed within the intestinal tissue.
Bestrophin expression and function in the human pancreatic duct cell line, CFPAC-1.
Winpenny et al., Norwich, United Kingdom. In J Physiol, 2009
Results provide evidence that the bestrophins are expressed in pancreatic duct cells and, more specifically, that hBest1 plays a role in the calcium activated chloride channels found in these cells.
Molecular evolution and functional divergence of the bestrophin protein family.
Weber et al., Regensburg, Germany. In Bmc Evol Biol, 2007
Most notably, significant functional divergence was found between bestrophin 4 and the other family members, as well as between bestrophin 2 and bestrophin 3. Site-specific profiles were established by posterior probability analysis revealing significantly divergent clusters mainly in two hydrophilic loops and a region immediately adjacent to the last predicted transmembrane domain.
Activation of bestrophin Cl- channels is regulated by C-terminal domains.
Hartzell et al., Atlanta, United States. In J Biol Chem, 2007
Bestrophins (VMD2, VMD2L1, VMD2L2, and VMD2L3) are a new family of anion channels.
Ca2+-activated Cl- current from human bestrophin-4 in excised membrane patches.
Yau et al., Baltimore, United States. In J Gen Physiol, 2006
Human Best4 chloride channels on excised membrane patches can be activated by free calcium (Ca2+) on the cytoplasmic side.
A short motif in the C-terminus of mouse bestrophin 3 [corrected] inhibits its activation as a Cl channel.
Hartzell et al., Atlanta, United States. In Febs Lett, 2006
Surprisingly, wild type mouse bestrophin-4 (mBest4) did not induce functional Cl channels when over-expressed in HEK293 cells.
Cloning and characterization of the murine Vmd2 RFP-TM gene family.
Weber et al., Würzburg, Germany. In Cytogenet Genome Res, 2003
VMD2, together with VMD2L1, VMD2L2 and VMD2L3, belong to a closely related gene family characterized by several transmembrane (TM) spanning helical domains and an invariant arginine, phenylalanine and proline (RFP) tripeptide motif, thus termed VMD2 RFP-TM.
Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family.
Weber et al., Würzburg, Germany. In Eur J Hum Genet, 2002
identified three novel VMD2-related human genes demonstrating a high degree of conservation in their respective RFP-TM domains
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