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Junctophilin 1

JP1, junctophilin, junctophilin type 1
Junctional complexes between the plasma membrane and endoplasmic/sarcoplasmic reticulum are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. The protein encoded by this gene is a component of junctional complexes and is composed of a C-terminal hydrophobic segment spanning the endoplasmic/sarcoplasmic reticulum membrane and a remaining cytoplasmic domain that shows specific affinity for the plasma membrane. This gene is a member of the junctophilin gene family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: JP2, CAN, HAD, JP-3, ACID
Papers on JP1
Combining confocal and single molecule localisation microscopy: A correlative approach to multi-scale tissue imaging.
New
Soeller et al., Auckland, New Zealand. In Methods, Nov 2015
Human cardiac tissue was first imaged at the nanoscale to identify macro-molecular membrane complexes containing the cardiac muscle proteins junctophilin (JPH) and the ryanodine receptor (RyR).
Ca²⁺ microdomains organized by junctophilins.
Review
New
Song et al., Kyoto, Japan. In Cell Calcium, Oct 2015
Junctophilin subtypes contribute to the formation and maintenance of JMCs by serving as a physical bridge between the plasma membrane and ER/SR membrane in different cell types.
Activity attenuates skeletal muscle fiber damage after ischemia and reperfusion.
New
Corona et al., Houston, United States. In Muscle Nerve, Oct 2015
Sedentary and active rats had a similar decline in neural-evoked (∼ 99%) and directly stimulated (∼ 70%) in vivo muscle torque, and a similar reduction in junctophilin 1. Active rats produced 19% and 15% greater neural-evoked torque compared with sedentary rats at 14 and 28 days postinjury, respectively, although the rate of recovery appeared similar.
Junctophilin 3 (JPH3) expansion mutations causing Huntington disease like 2 (HDL2) are common in South African patients with African ancestry and a Huntington disease phenotype.
New
Margolis et al., Johannesburg, South Africa. In Am J Med Genet B Neuropsychiatr Genet, Oct 2015
A CAG/CTG repeat expansion in the junctophilin-3 (JPH3) gene on chromosome 16q24.2
Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.
New
Rossi et al., Siena, Italy. In J Muscle Res Cell Motil, Oct 2015
The muscle-specific junctophilin isoforms (JPH1 and JPH2) are anchored to the j-SR with a trans-membrane segment present at the C-terminus and are capable to bind the sarcolemma with a series of phospholipid-binding motifs localized at the N-terminus.
Medicinal effect and its JP2/RyR2-based mechanism of Smilax glabra flavonoids on angiotensin II-induced hypertrophy model of cardiomyocytes.
New
Chen et al., Hangzhou, China. In J Ethnopharmacol, Aug 2015
Such effect could be mediated by the modulation of intracellular Ca(2+) flux in myocardial cells, in which junctophilin-2 (JP2) and ryanodine receptor 2 (RyR2) play an important role.
Nanoscale analysis of ryanodine receptor clusters in dyadic couplings of rat cardiac myocytes.
New
Soeller et al., Auckland, New Zealand. In J Mol Cell Cardiol, Mar 2015
Dual-colour dSTORM revealed high co-localisation between the cardiac junctional protein junctophilin-2 (JPH2) and RyR clusters that confirmed that the majority of the RyR clusters observed are dyadic.
Dependence of cardiac transverse tubules on the BAR domain protein amphiphysin II (BIN-1).
Trafford et al., Manchester, United Kingdom. In Circ Res, 2015
Conversely, junctophilin 2 levels did not show interchamber differences in the rat and ferret nor did they change in HF in the sheep or ferret.
Eps 15 Homology Domain (EHD)-1 Remodels Transverse Tubules in Skeletal Muscle.
McNally et al., Omaha, United States. In Plos One, 2014
The disorganized T-tubule structures in Ehd1-heterozygous muscle were accompanied by marked elevation of the T-tubule-associated protein DHPR and reduction of the triad linker protein junctophilin 2, reflecting defective triads.
Reduced junctional Na+/Ca2+-exchanger activity contributes to sarcoplasmic reticulum Ca2+ leak in junctophilin-2-deficient mice.
Wehrens et al., Auckland, New Zealand. In Am J Physiol Heart Circ Physiol, 2014
Expression silencing of junctophilin-2 (JPH2) in mouse heart leads to ryanodine receptor type 2 (RyR2)-mediated sarcoplasmic reticulum (SR) Ca(2+) leak and rapid development of heart failure.
Emerging roles of junctophilin-2 in the heart and implications for cardiac diseases.
Review
Wehrens et al., Houston, United States. In Cardiovasc Res, 2014
In a little over a decade, junctophilin-2 (JPH2) has become recognized as a cardiac structural protein critical in forming junctional membrane complexes (JMCs), which are subcellular domains essential for excitation-contraction coupling within the heart.
The junctophilin family of proteins: from bench to bedside.
Review
Wehrens et al., Houston, United States. In Trends Mol Med, 2014
Within skeletal and cardiac muscle, junctophilin 1 and junctophilin 2, respectively, couple sarcolemmal and intracellular calcium channels.
Microarchitecture of the dyad.
Review
Moore et al., Vancouver, Canada. In Cardiovasc Res, 2013
The essential role of proteins, such as junctophilin-2, calsequestrin, triadin, and junctin that maintain both the functional and structural integrity of the dyad have recently been elucidated giving a new mechanistic understanding of heart diseases, such as arrhythmias, hypertension, failure, and sudden cardiac death.
Junctophilin 1 and 2 proteins interact with the L-type Ca2+ channel dihydropyridine receptors (DHPRs) in skeletal muscle.
GeneRIF
Sorrentino et al., Siena, Italy. In J Biol Chem, 2012
JP1 and JP2 can facilitate the assembly of DHPR with other proteins of the excitation-contraction coupling machinery
Molecular architecture of Ca2+ signaling control in muscle and heart cells.
Review
Ma et al., United States. In Channels (austin), 2011
Here we summarize the functions of three key molecules that are located in the junctional membrane complex of skeletal and cardiac muscle cells: junctophilin as a "glue" that physiologically links the SR membrane to the sarcolemmal membrane for formation of the junctional membrane framework, mitsugumin29 as a muscle-specific synaptophysin family protein that contributes to maintain the coordinated Ca2+ signaling in skeletal muscle, and TRIC as a novel cation-selective channel located on the SR membrane that provides counter-ion current during the rapid process of Ca2+ release from the SR.
Impaired Orai1-mediated resting Ca2+ entry reduces the cytosolic [Ca2+] and sarcoplasmic reticulum Ca2+ loading in quiescent junctophilin 1 knock-out myotubes.
GeneRIF
Eltit et al., Boston, United States. In J Biol Chem, 2011
an important fraction of resting plasmalemmal Ca(2+) permeability is mediated by the Orai1 pathway, which contributes to the control of [Ca(2+)](rest) and resting Ca(2+) stores and that this pathway is defective in JP1 KO myotubes
Junctophilin damage contributes to early strength deficits and EC coupling failure after eccentric contractions.
GeneRIF
Ingalls et al., Atlanta, United States. In Am J Physiol Cell Physiol, 2010
Skeletal muscle JP1/2 damage is significantly associated with early (0-3 days) strength deficits after performance of eccentric contractions.
Junctophilin-mediated channel crosstalk essential for cerebellar synaptic plasticity.
GeneRIF
Takeshima et al., Tokyo, Japan. In Embo J, 2007
Junctophilins support the Ca(2+)-mediated communication between voltage-gated Ca(2+) channels, which modulates the excitability of Purkinje cells and is fundamental to cerebellar long-term depression and motor functions.
Coexpression of junctophilin type 3 and type 4 in brain.
GeneRIF
Takeshima et al., Sendai, Japan. In Brain Res Mol Brain Res, 2003
We report a novel Junctophilin subtype, JP-4, encoded in the human (chromosome 14q11.1) and mouse (chromosome 14C1-2) genomes. JP-4 shares characteristic structural features with other JP subtypes, and is found in the brain.
A repeat expansion in the gene encoding junctophilin-3 is associated with Huntington disease-like 2.
Impact
Margolis et al., Baltimore, United States. In Nat Genet, 2001
We now report the cloning of this expansion and its localization to a variably spliced exon of JPH3 (encoding junctophilin-3), a gene involved in the formation of junctional membrane structures.
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