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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Leucine rich repeat containing 8 family, member A

LRRC8
This gene encodes a protein belonging to the leucine-rich repeat family of proteins, which are involved in diverse biological processes, including cell adhesion, cellular trafficking, and hormone-receptor interactions. This family member is a putative four-pass transmembrane protein that plays a role in B cell development. Defects in this gene cause autosomal dominant non-Bruton type agammaglobulinemia, an immunodeficiency disease resulting from defects in B cell maturation. Multiple alternatively spliced transcript variants, which encode the same protein, have been identified for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, LRRC8D, V1a, CAN, iMpact
Papers on LRRC8
Cellular volume regulation by anoctamin 6: Ca(2+), phospholipase A2 and osmosensing.
New
Kunzelmann et al., Regensburg, Germany. In Pflugers Arch, Feb 2016
Thereby, it may support the function of LRRC8 proteins.
Distinct pharmacological and molecular properties of the acid-sensitive outwardly rectifying (ASOR) anion channel from those of the volume-sensitive outwardly rectifying (VSOR) anion channel.
New
Okada et al., Tokyo, Japan. In Pflugers Arch, Feb 2016
Although leucine-rich repeats containing 8A (LRRC8A) was recently found to be an essential component of VSOR anion channels, the possibility of an LRRC8 family member serving as a component of ASOR anion channels has not been examined.
Biophysics and Physiology of the Volume-Regulated Anion Channel (VRAC)/Volume-Sensitive Outwardly Rectifying Anion Channel (VSOR).
New
Nilius et al., Copenhagen, Denmark. In Pflugers Arch, Feb 2016
Members of this distantly pannexin-1-related protein family form heteromers, and in addition to LRRC8A, at least another LRRC8 family member is required for the formation of a functional VRAC.
Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs.
New
Jentsch et al., Berlin, Germany. In Embo J, Jan 2016
We show that the loss of subunits LRRC8A and LRRC8D of the heteromeric LRRC8 volume-regulated anion channels (VRACs) increased resistance to clinically relevant cisplatin/carboplatin concentrations.
VRAC: molecular identification as LRRC8 heteromers with differential functions.
New
Voss et al., Berlin, Germany. In Pflugers Arch, Jan 2016
In 2014, in a final breakthrough, two groups independently identified LRRC8A as indispensable component of VRAC.
Volume-regulated anion channel-a frenemy within the brain.
New
Mongin, Albany, United States. In Pflugers Arch, Jan 2016
Two pioneer publications identified VRAC as the heterohexamer formed by the leucine-rich repeat-containing 8 (LRRC8) proteins.
Calcium homeostasis modulator (CALHM) ion channels.
New
Foskett et al., Philadelphia, United States. In Pflugers Arch, Dec 2015
Through convergent evolution, CALHM has structural features that are reminiscent of connexins and pannexins/innexins/LRRC8 (volume-regulated anion channel (VRAC)) gene families, including four transmembrane helices with cytoplasmic amino and carboxyl termini.
The volume-regulated anion channel is formed by LRRC8 heteromers – molecular identification and roles in membrane transport and physiology.
Review
New
Stauber, In Biol Chem, Sep 2015
Despite many efforts, the molecular identity of VRAC had remained elusive for decades, until the recent discovery of heteromers of LRRC8A with other LRRC8 family members as an essential VRAC component.
TMEM16, LRRC8A, bestrophin: chloride channels controlled by Ca(2+) and cell volume.
Review
New
Kunzelmann, Regensburg, Germany. In Trends Biochem Sci, Sep 2015
Recent years, however, have shown remarkable progress, and these channels have been identified as TMEM16A (anoctamin 1), LRRC8A (swell 1), and bestrophin 1 (BEST1), and structural information is already available for the Ca(2+)-activated channels bestrophin and TMEM16.
The identification of a volume-regulated anion channel: an amazing Odyssey.
Review
New
Nilius et al., Copenhagen, Denmark. In Acta Physiol (oxf), Apr 2015
Finally, we describe properties of the LRRC8 proteins, highlight some features of the LRRC8A knockout mouse and discuss the impact of the discovery of LRRC8 as VRAC on future research.
Regulation of vascular tone and arterial blood pressure: role of chloride transport in vascular smooth muscle.
Review
New
Ehmke et al., Jena, Germany. In Pflugers Arch, Mar 2015
Additional proteins associated with Cl(-) flux in vascular smooth muscle are bestrophins, which modulate vasomotion, the volume-activated LRRC8, and the cystic fibrosis transmembrane conductance regulator (CFTR).
TMC8 (EVER2) attenuates intracellular signaling by Zn2+ and Ca2+ and suppresses activation of Cl- currents.
Kunzelmann et al., Regensburg, Germany. In Cell Signal, 2014
On the contrary, TMC8 was found to be localized in the endoplasmic reticulum (ER), where it inhibited receptor mediated Ca(2+) release, activation of Ano1 and volume regulated LRRC8-related Cl(-) currents.
LRRC8A protein is indispensable for swelling-activated and ATP-induced release of excitatory amino acids in rat astrocytes.
Mongin et al., Albany, United States. In J Physiol, 2014
Two recent studies discovered that LRRC8 gene family members encode heteromeric VRAC composed of LRRC8A plus LRRC8B-E, which mediate swelling-activated Cl(-) currents and taurine release in human non-neural cells (Z.
The protein synthesis inhibitor blasticidin s enters mammalian cells via leucine-rich repeat-containing protein 8D.
Ploegh et al., Cambridge, United States. In J Biol Chem, 2014
Leucine-rich repeat-containing 8 (LRRC8) proteins have been identified as putative receptors involved in lymphocyte development and adipocyte differentiation.
Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC.
Impact
Jentsch et al., Berlin, Germany. In Science, 2014
LRRC8A formed heteromers with other LRRC8 multispan membrane proteins.
LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins.
GeneRIF
Hara et al., Suita, Japan. In Febs Lett, 2004
identified four genes, named TA-LRRP, AD158, LRRC5, and FLJ23420, as unknown LRRC8-like genes
A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans.
GeneRIF
Hara et al., Suita, Japan. In J Clin Invest, 2003
LRRC8 is required for B cell development.
Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro.
GeneRIF
Ohara et al., Kisarazu, Japan. In Dna Res, 2000
Includes the cloning of this gene, designated as KIAA1437.
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