BLOCK-iT™ RNAi Express
READY, CLICK and GO: Fast and easy online ordering of bench-tested Validated Stealth RNAi™ siRNA, ready-to-order Stealth Select RNAi™ siRNA, bench-tested BLOCK-iT™ Pol II miR Validated miRNA Vector Duopaks.      RNAi Express Options:  Search By ID/Keyword Browse By Pathways Browse By Gene Families
Calcium Signaling Pathway Calcium (Ca2+) is a potent signaling molecule that is involved in many different cellular responses. Following receptor activation, members of the phosphatidylinositol-specific PLC (PI-PLC) family hydrolyze phosphatidylinositol 4,5 bisphosphate (PIP2) to generate inositol 1,4,5 triphosphate (IP3) and diacylglycerol (DAG). IP3 initiates the release of intracellular Ca2+ from the endoplasmic reticulum. Extracellular Ca2+ influx is subsequently triggered through the activation of Ca2+ release activated Ca2+ channels (CRAC) by a process called capacitative Ca2+ entry. Calmodulin, an intracellular Ca2+ sensor, binds to Ca2+ and activates the serine-threonine phosphatase calcineurin. Calcineurin dephosphorylates serine residues on the N-terminus of NFATc transcription factors activating nuclear translocation. In the nucleus, NFATc proteins bind to DNA in conjunction with other associated transcription factors (NFATn) to regulate gene expression. Another protein family that is regulated by Ca2+ and DAG is protein kinase C (PKC). PKC is a serine-threonine kinase that regulates many different cellular processes including cell cycle, proliferation, differentiation, cytoskeletal organization, migration, and apoptosis. The PKC enzyme family includes three subgroups corresponding to conventional (α1,β1,β2,γ), novel (δ,ε,η,θ,μ), and atypical isoforms (ζ,λ). Although only the conventional PKC isoforms are activated by Ca2+, both the conventional and novel PKC isoforms are activated by DAG.     Calcium Signaling Pathway BLOCK-iT™ Validated Stealth RNAi Phosphatidylinositol-PLC Calmodulin Calcineurin NFAT Protein Kinase C   References 1. Crabtree, G.R. & Olson E.N. NFAT signaling: choreographing the social lives of cells. Cell 109, S67-S79 (2002). 2. Graef, I.A., Chen, F., Crabtree, G.R. NFAT signaling in vertebrate development. Curr. Opin. Genet. Dev. 11, 505-512 (2001). 3. Hogan, P.G. et al. Transcriptional regulation by calcium, calcineurin, and NFAT. Genes Dev. 17, 2205-2232 (2003). 4. Mellor, H. & Parker, P.J. The extended protein kinase C superfamily. Biochem. J. 332, 281-292 (1998). 5. Rebecchi, M.J. & Pentyala, S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80, 1291-1335 (2000). 6. Spitaler, M. & Cantrell, D.A. Protein kinase C and beyond. Nat. Immunol. 8, 785-790 (2004). 7. Taylor, C.J. Controlling calcium entry. Cell 111, 767-769 (2002).