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G-Protein Signaling Through Tubby Proteins
It is shown that tubby functions in signal transduction from heterotrimeric GTP-binding protein (G protein)–coupled receptors, providing a direct link between G-protein signaling and the regulation of gene expression. Expand
Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation.
It is found that phosphorylation of a cardiac skinned muscle preparation by PKA results in a decrease in the Ca2+ sensitivity of muscle contraction, which can account for the faster relaxation seen in the inotropic response of the heart to catecholamines. Expand
Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin.
Analysis of the CT deletion and point-mutation variants of gp600/megalin by the two-hybrid system revealed that the third PsiXNPXY motif is most probably involved in this interaction with Dab2, the first known transmembrane receptor that interacts with the cytosolic protein Dab 2. Expand
Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy.
Changes in the Ca(2+) regulation of force development caused by these mutations would likely cause altered contractility and contribute to the development of FHC. Expand
Five-transmembrane domains appear sufficient for a G protein-coupled receptor: functional five-transmembrane domain chemokine receptors.
  • K. Ling, P. Wang, +6 authors G. Pei
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 6 July 1999
It is indicated that five-TM domains, at least in the case of CCR5 and CXCR4, appear to meet the minimum structural requirements for a functional GPCR and suggests possible existence of functional five- TM GPCRs in nature during evolution. Expand
Molecular Cloning of Human Plasma Membrane Phospholipid Scramblase
Quantitative immunoblotting revealed an approximately 10-fold higher abundance of PL scramblase in platelet than in erythrocyte, consistent with apparent increased PL scrambleblase activity of the platelet plasma membrane. Expand
Functional calcium release channel formed by the carboxyl-terminal portion of ryanodine receptor.
The results show that the C-terminal portion of RyR contains structures sufficient to form a functional Ca2+ release channel, but the N-terminAL portion ofRyR also affects the ion-conduction and calcium-dependent regulation of the Ca2+, which inactivates at millimolar Ca2+. Expand
Transcriptional control of the human plasma membrane phospholipid scramblase 1 gene is mediated by interferon-alpha.
Analysis of 5' flanking genomic sequence in reporter constructs showed that transcriptional control of PLSCR1 was entirely regulated by a single IFN-stimulated response element located in the first exon, indicating that remodeling of the cell surface requires both exposure to IFN and a second yet-to-be identified event to stimulate plasma membrane phospholipid scramblase activity and to mobilize phosphatidylserine to thecell surface. Expand
A Direct Regulatory Role for Troponin T and a Dual Role for Troponin C in the Ca2+ Regulation of Muscle Contraction (*)
The results suggest that TnT reconstitutes native Ca2+ sensitivity via direct interaction with TnC, which would have a dual role: 1) release of the ATPase inhibition by TnI and 2) activation ofThe ATPase through interaction withTnT. Expand
Phosphorylation of Both Serine Residues in Cardiac Troponin I Is Required to Decrease the Ca2+ Affinity of Cardiac Troponin C (*)
The phosphorylation of cardiac muscle troponin I at two adjacent N-terminal serine residues by cAMP-dependent protein kinase (PKA) has been implicated in the inotropic response of the heart to β-agonists and suggests that one of the serines (23) may be constitutively phosphorylated and that serine 22 may be functionally more important. Expand