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Voltage-gated Ca(2+) and Na+ channels have 4 homologous domains, each containing 6 transmembrane segments, S1 to S6. Additionally we are shipping Two Pore Segment Channel 1 Antibodies (18) and many more products for this protein.
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TPC1 role in the systemic response to salt stress
Structure-function analysis of the Arabidopsis TPC1 channel in planta confirmed that helix S10 (show PSMD6 Proteins) operates as the major voltage-sensing site, with Glu450 and Glu478 identified as possible ion-pair partners for voltage-sensing Arg537.
The domain architecture of TPC1 has been discussed.
This study discovered that the dimerization of a predicted helix within the carboxyl-terminus is essential for the activity of TPC1.
crystal structure of TPC1 from Arabidopsis thaliana at 2.87 A resolution as a basis for understanding ion permeation, channel activation, the location of voltage-sensing domains and regulatory ion-binding sites
crystal structure of a vacuolar two-pore channel from Arabidopsis thaliana, AtTPC1, which functions as a homodimer
The SV channel fou2 mutation in TCP1 altered sensitivity to luminal Ca2 (show CA2 Proteins)+ levels.
TPC1 contains a N-terminal dileucine motif (EDPLI) critical for vacuolar targeting
TPC1 has a role in maintaining differential K and Ca storage across the leaf; it releases Ca2 (show CA2 Proteins)+ from epidermal and bundle sheath cell vacuoles to maintain low [Ca]vac.
EF-hand 1 (show HAND1 Proteins) modulates the Ca2 (show CA2 Proteins)+-sensitivity of TPC1, whereas EF-hand 2 (show HAND2 Proteins) is essential for the Ca2 (show CA2 Proteins)+-dependent channel opening.
TPC1 and TPC2 (show TPCN2 Proteins) were found to be essential for appropriate basal and induced autophagic flux in cardiomyocytes.
The results confirmed the altered expression of HFABP (show FABP3 Proteins), a key fatty acid transport protein (show CD36 Proteins), and of enolase and PGK1 (show PGK1 Proteins), the key enzymes in the glycolytic process
Mice lacking the endo-lysosomal TPC1 were protected from myocardial ischemia reperfusion injury.
Genetic ablation of endolysosomal TPC1 or TPC2 (show TPCN2 Proteins) channels attenuates glucose- and sulfonylurea-induced membrane currents, depolarization, cytoplasmic Ca2 (show CA2 Proteins)+ signals, and insulin (show INS Proteins) secretion in pancreatic beta cells.
It was concluded that Tpcn1/2(-/-) mice show mature-onset obesity due to reduced lipid availability and use, and a defect in beta-adrenergic receptor signaling, leading to impaired thermogenic activity, in brown adipose tissue.
Results report the existence of a novel, alternative variant isoform of Tpcn1, termed Tpcn1B, resulting from an alternative promoter and giving rise to a TPC1B protein with an N-terminal truncation relative to the sequence of the TPC1A.
NAADP and the two-pore calcium channel TPC1 participate in the acrosome reaction in mammalian spermatozoa.
TPC1 is a member of a new family of voltage-gated Na(+) channels that senses pH changes and confers electrical excitability to organelles.
We find alterations in two-pore calcium channel protein expression, with loss of presenilin preventing the formation of a high molecular weight species of TPC1 and TPC2 (show TPCN2 Proteins).
Study identifies an endolysosomal ATP-sensitive Na channel - a complex formed by two-pore channels TPC1 and TPC2 (show TPCN2 Proteins); channel complex detects nutrient status, becomes constitutively open upon nutrient removal and mTOR (show FRAP1 Proteins) translocation off the lysosomal membrane, and controls the lysosome's membrane potential, pH stability, and amino acid homeostasis.
These findings indicate potential differential regulation of signaling processes by TPC1 and TPC2 (show TPCN2 Proteins) in breast cancer cells.
Studies suggest that both two-pore channels TPC1 and TPC2 (show TPCN2 Proteins) as nicotinic acid adenine dinucleotide phosphate (NAADP) targets.
The TPC1 was shown to interact with citron kinase, with TPC1 overexpression affecting RhoA activity and myosin light chain phosphorylation levels in cytokinesis.
NAADP induced marked Ca(2 (show CA2 Proteins)+) transients in HEK293 cells that stably coexpressed hTPC2 with hTPC1 or cTPC3, but failed to evoke any such response in cells that coexpressed interacting hTPC2 and rTPC3 subunits
TPC2 (show TPCN2 Proteins), but not TPC1, caused a proliferation of endolysosomal structures, dysregulating intracellular trafficking, and cellular pigmentation.
TPC1 and TPC2 (show TPCN2 Proteins) proteins play a key role in Ebola virus infection and may be effective targets for antiviral therapy.
NAADP triggers H+ release from lysosomes and endolysomes through activation of TPC1, but that the Ca2 (show CA2 Proteins)+ -releasing ability of TPC1 will depend on the ionic composition of the acidic stores
The concerted regulation of TPC1 activity by luminal Ca(2 (show CA2 Proteins)+) and by membrane potential thus provides a potential mechanism to explain NAADP-induced Ca(2 (show CA2 Proteins)+) oscillations.
OsTPC1 plays a crucial role in TvX-induced Ca(2 (show CA2 Proteins)+) influx as a plasma membrane Ca(2 (show CA2 Proteins)+)-permeable channel consequently required for the regulation of phytoalexin biosynthesis
Voltage-gated Ca(2+) and Na+ channels have 4 homologous domains, each containing 6 transmembrane segments, S1 to S6. TPCN1 is similar to these channels, but it has only 2 domains containing S1 to S6 (Ishibashi et al., 2000
two pore calcium channel protein 1
, voltage-dependent calcium channel protein TPC1
, two-pore channel 1
, two-pore segment channel 1
, two pore channel 1
, voltage-gated Ca channel