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Chloride channel, nucleotide-sensitive, 1A

ICln, pICln, CLNS1A
This gene encodes a protein that functions in multiple regulatory pathways. The encoded protein complexes with numerous cytosolic proteins and performs diverse functions including regulation of small nuclear ribonucleoprotein biosynthesis, platelet activation and cytoskeletal organization. The protein is also found associated with the plasma membrane where it functions as a chloride current regulator. Pseudogenes of this gene are found on chromosomes 1, 4 and 6. [provided by RefSeq, Feb 2009] (from NCBI)
Top mentioned proteins: CAN, ACID, PRMT5, SmaI, ClC-3
Papers on ICln
Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.
Fischer et al., Würzburg, Germany. In Embo J, Aug 2015
We uncover a stepwise and ordered formation of distinct Sm protein complexes on the PRMT5 complex, which is facilitated by the assembly chaperone pICln.
The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.
Shechter et al., Anchorage, United States. In Cell Mol Life Sci, Jun 2015
PRMT5 also directly associates with a range of other protein factors, including pICln, Menin, CoPR5 and RioK1 that may alter its subcellular localization and protein substrate selection.
The influence of experimental administration of low zearalenone doses on the expression of Th1 and Th2 cytokines and on selected subpopulations of lymphocytes in intestinal lymph nodes.
Żmigrodzka et al., In Pol J Vet Sci, 2014
The aim of this study was to characterize the immune response taking place in ileocecal lymph nodes (ICLN) in control (n=15) and zearalenone (ZEN)-treated (n=15) pigs.
Reduction of Salmonella enterica serovar typhimurium DT104 infection in experimentally challenged weaned pigs fed a lactobacillus-fermented feed.
Gong et al., Changsha, China. In Foodborne Pathog Dis, 2014
were detected in both ileocecal lymph nodes (ICLN) and spleens from all pigs on BD, NF, and LC-F, but only 50% of spleens from pigs on LZ-F.
Characterization and in vivo functional analysis of the Schizosaccharomyces pombe ICLN gene.
Bordonné et al., Montpellier, France. In Mol Cell Biol, 2014
During the early steps of snRNP biogenesis, the survival motor neuron (SMN) complex acts together with the methylosome, an entity formed by the pICln protein, WD45, and the PRMT5 methyltransferase.
Microbiomes of unreactive and pathologically altered ileocecal lymph nodes of slaughter pigs.
Schmitz-Esser et al., Vienna, Austria. In Appl Environ Microbiol, 2014
Correlation-based networks revealed interactions among OTUs in all ICLN groups, and discriminant analyses depicted discrimination in response to pathological alterations.
ICln: a new regulator of non-erythroid 4.1R localisation and function.
Rodighiero et al., Milano, Italy. In Plos One, 2013
We studied the interaction between two potential hub proteins, ICln and 4.1R (in the form of its two splicing variants 4.1R80 and 4.1R135), which are involved in such crucial cell functions as proliferation, RNA processing, cytoskeleton organisation and volume regulation.
Structural basis of assembly chaperone- mediated snRNP formation.
Fischer et al., Würzburg, Germany. In Mol Cell, 2013
The assembly chaperone pICln initially mediates the formation of an otherwise unstable pentameric Sm protein unit.
The molecular and functional interaction between ICln and HSPC038 proteins modulates the regulation of cell volume.
Paulmichl et al., Salzburg, Austria. In J Biol Chem, 2011
functional interaction between ICln and HSPC038
RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.
Grimmler et al., Würzburg, Germany. In J Biol Chem, 2011
RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.
An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.
Fischer et al., Würzburg, Germany. In Cell, 2008
We show that pICln, a component of the PRMT5 complex, induces the formation of an otherwise unstable higher-order Sm protein unit.
Roles of volume-sensitive chloride channel in excitotoxic neuronal injury.
Okada et al., Okazaki, Japan. In J Neurosci, 2007
1st demonstration of VSOR Cl- channel expression in somatosensory pyramidal neurons. It is the major anionic pathway for varicosity recovery after NMDA & for persistent NMDA-induced varicosity formation leading to necrosis in cortical neurons.
Involvement of potassium and chloride channels and other transporters in volume regulation by spermatozoa.
Yeung et al., Münster, Germany. In Curr Pharm Des, 2006
The evidence for the presence of ion channels probably responsible for regulatory volume decreases in spermatozoa is reviewed here that implicate voltage-gated potassium channels (especially Kv1.5 (KCNA5), minK (KCNE1) and TASK2 (KCNK5)) and the chloride channels CLCN3 and CLNS1A.
The ICln interactome.
Paulmichl et al., Innsbruck, Austria. In Acta Physiol (oxf), 2006
Here, we describe the present knowledge of the ICln interactome.
New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium.
Gascard et al., Berkeley, United States. In Front Biosci, 2005
Specifically, we will focus on renal 4.1 protein interactions with beta amyloid precursor protein (beta-APP), 14-3-3 proteins, and the cell swelling-activated chloride channel pICln.
Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.
Schümperli et al., Bern, Switzerland. In J Biol Chem, 2005
Lsm10 and Lsm11, which replace the Sm proteins D1 and D2 in the histone RNA processing U7 snRNPs, associate with pICln in vitro and in vivo without receiving sDMA modifications and with PRMT5 and SMN complexes
ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4.
Paulmichl et al., Innsbruck, Austria. In J Biol Chem, 2005
Data show that ICln159, a truncated ICln mutant, belongs to the pleckstrin homology (PH) domain family of proteins and interacts with LSm4, a protein involved in splicing and mRNA degradation.
Structure and function of the ion channel ICln.
Paulmichl et al., Innsbruck, Austria. In Cell Physiol Biochem, 1999
Several proteins are discussed as the channel forming IClswell, i.e. phospholemman, p-glycoprotein, CLC-3 and ICln.
Molecular identification of a volume-regulated chloride channel.
Horowitz et al., Reno, United States. In Nature, 1997
Although three putative chloride channel proteins expressed from cloned genes (P-glycoprotein, pICln and ClC-2 ) have been proposed to be the molecular equivalent of ICl.vol, neither P-glycoprotein nor pICln is thought to be a chloride channel or part thereof, and the properties of expressed ClC-2 channels differ from native ICl.vol.
Molecular characterization of a swelling-induced chloride conductance regulatory protein, pICln.
Clapham et al., Rochester, United States. In Cell, 1994
Expression in Xenopus oocytes of a novel protein, pICln, activated a chloride conductance.
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