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Orai proteins interact with TRPC channels and confer responsiveness to store depletion
It is proposed that Orai proteins by interacting with TRPCs act as regulatory subunits that confer STIM1-mediated store depletion sensitivity to these channels.
Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE/Icrac channels
It is proposed that SOCE/Icrac channels are composed of heteromeric complexes that include TRPCs and Orai proteins, and functional interaction between ROCE and SOCE components is shown.
Structure of a signal transduction regulator, RACK1, from Arabidopsis thaliana
The first crystal structure of a Rack1 protein, RACK1 isoform A from Arabidobsis thaliana, is presented, at 2.4 Å resolution, as a C‐terminal fusion of the maltose binding protein, which implicates highly conserved surface residues that could play critical roles in protein–protein interactions and reveals the surface location of proposed post‐transcriptionally modified residues.
Voltage-activated calcium channels that must be phosphorylated to respond to membrane depolarization.
Evidently the dihydropyridine-sensitive class of voltage-activated calcium channels must be phosphorylated in order to open when the membrane is depolarized, which provides a simple framework for understanding the modulation of calcium channel gating by neurotransmitters, calcium ions, and diHydropyridines.
Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormone.
TRbeta signaling through PI3K provides a molecular explanation for the essential role of thyroid hormone in human brain development and adult lipid metabolism.
Stimulation of Kv1.3 Potassium Channels by Death Receptors during Apoptosis in Jurkat T Lymphocytes*
Caspase-dependent stimulation of potassium channels by the Fas receptor increases Kv1.3 channel activity through the same canonical apoptotic signaling cascade that is required for potassium efflux, cell shrinkage, and apoptosis.
Purification of a Fatty Acid-stimulated Protein-serine/threonine Phosphatase from Bovine Brain and Its Identification as a Homolog of Protein Phosphatase 5*
The results suggest that protein phosphatase 5 may be regulated in vivo by a lipid second messenger or another endogenous activator.
Stable Activation of Single Ca2+ Release-activated Ca2+ Channels in Divalent Cation-free Solutions*
The regulation of store-operated, calcium-selective channels in the plasma membrane of rat basophilic leukemia cells (RBL-2H3 m1), an immortalized mucosal mast cell line, was studied at the
Calcium-dependent inactivation of the dihydropyridine-sensitive calcium channels in GH3 cells
The inactivation of the dihydropyridine-sensitive calcium channels in GH3 cells only occurs when membrane depolarization leads to calcium ion entry and intracellular accumulation.