Table of Contents Author Guidelines Submit a Manuscript
International Journal of Endocrinology
Volume 2011, Article ID 746482, 13 pages
http://dx.doi.org/10.1155/2011/746482
Research Article

The Involvement of Ser1898 of the Human L-Type Calcium Channel in Evoked Secretion

Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 919104, Israel

Received 3 July 2011; Accepted 17 August 2011

Academic Editor: Maria L. Dufau

Copyright © 2011 Niv Bachnoff et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. H. Reuter, “Calcium channel modulation by β-adrenergic neurotransmitters in the heart,” Experientia, vol. 43, no. 11-12, pp. 1173–1175, 1987. View at Google Scholar · View at Scopus
  2. A. C. Dolphin, “L-type calcium channel modulation,” Advances in Second Messenger and Phosphoprotein Research, vol. 33, pp. 153–177, 1999. View at Google Scholar · View at Scopus
  3. K. Nunoki, V. Florio, and W. A. Catterall, “Activation of purified calcium channels by stoichiometric protein phosphorylation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 17, pp. 6816–6820, 1989. View at Google Scholar · View at Scopus
  4. W. A. Catterall, “Structure and regulation of voltage-gated Ca2+ channels,” Annual Review of Cell and Developmental Biology, vol. 16, pp. 521–555, 2000. View at Publisher · View at Google Scholar · View at Scopus
  5. B. P. Bean, M. C. Nowycky, and R. W. Tsien, “β-Adrenergic modulation of calcium channels in frog ventricular heart cells,” Nature, vol. 307, no. 5949, pp. 371–375, 1984. View at Google Scholar · View at Scopus
  6. T. F. Mcdonald, S. Pelzer, W. Trautwein, and D. J. Pelzer, “Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells,” Physiological Reviews, vol. 74, no. 2, pp. 365–507, 1994. View at Google Scholar · View at Scopus
  7. C. A. Artalejo, M. K. Dahmer, R. L. Perlman, and A. P. Fox, “Two types of Ca2+ currents are found in bovine chromaffin cells: facilitation is due to the recruitment of one type,” Journal of Physiology, vol. 432, pp. 681–707, 1991. View at Google Scholar · View at Scopus
  8. C. R. Artalejo, S. Rossie, R. L. Perlman, and A. P. Fox, “Voltage-dependent phosphorylation may recruit Ca2+ current facilitation in chromaffin cells,” Nature, vol. 358, no. 6381, pp. 63–66, 1992. View at Publisher · View at Google Scholar · View at Scopus
  9. E. T. Kavalali, K. S. Hwang, and M. R. Plummer, “cAMP-dependent enhancement of dihydropyridine-sensitive calcium channel availability in hippocampal neurons,” Journal of Neuroscience, vol. 17, no. 14, pp. 5334–5348, 1997. View at Google Scholar · View at Scopus
  10. A. Sculptoreanu, E. Rotman, M. Takahashi, T. Scheuer, and W. A. Catterall, “Voltage-dependent potentiation of the activity of cardiac L-type calcium channel α1 subunits due to phosphorylation by cAMP-dependent protein kinase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 21, pp. 10135–10139, 1993. View at Publisher · View at Google Scholar · View at Scopus
  11. D. T. Yue, S. Herzig, and E. Marban, “β-Adrenergic stimulation of calcium channels occurs by potentiation of high-activity gating modes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 2, pp. 753–757, 1990. View at Google Scholar · View at Scopus
  12. D. M. Bers, “Cardiac excitation-contraction coupling,” Nature, vol. 415, no. 6868, pp. 198–205, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. M. A. Davare, V. Avdonin, D. D. Hall et al., “A β2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav 1.2,” Science, vol. 293, no. 5527, pp. 98–101, 2001. View at Publisher · View at Google Scholar · View at Scopus
  14. K. S. De Jongh, B. J. Murphy, A. A. Colvin, J. W. Hell, M. Takahashi, and W. A. Catterall, “Specific phosphorylation of a site in the full-length form of the α1 subunit of the cardiac L-type calcium channel by adenosine 3-5-cyclic monophosphate-dependent protein kinase,” Biochemistry, vol. 35, no. 32, pp. 10392–10402, 1996. View at Publisher · View at Google Scholar · View at Scopus
  15. J. Mitterdorfer, M. Froschmayr, M. Grabner, F. F. Moebius, H. Glossmann, and J. Striessnig, “Identification of PK-A phosphorylation sites in the carboxyl terminus of L-type calcium channel α1 subunits,” Biochemistry, vol. 35, no. 29, pp. 9400–9406, 1996. View at Publisher · View at Google Scholar · View at Scopus
  16. P. C. Gray, J. D. Scott, and W. A. Catterall, “Regulation of ion channels by cAMP-dependent protein kinase and A-kinase anchoring proteins,” Current Opinion in Neurobiology, vol. 8, no. 3, pp. 330–334, 1998. View at Publisher · View at Google Scholar · View at Scopus
  17. J. T. Hulme, R. E. Westenforoek, T. Scheuer, and W. A. Catterall, “Phosphorylation of serine 1928 in the distal C-terminal domain of cardiac Cav1.2 channels during β1-adrenergic regulation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 44, pp. 16574–16579, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. J. W. Hell, C. T. Yokoyama, S. T. Wong, C. Warner, T. P. Snutch, and W. A. Catterall, “Differential phosphorylation of two size forms of the neuronal class C L- type calcium channel α1 subunit,” The Journal of Biological Chemistry, vol. 268, no. 26, pp. 19451–19457, 1993. View at Google Scholar · View at Scopus
  19. T. Perets, Y. Blumenstein, E. Shistik, I. Lotan, and N. Dascal, “A potential site of functional modulation by protein kinase A in the cardiac Ca2+ channel α1c subunit,” FEBS Letters, vol. 384, no. 2, pp. 189–192, 1996. View at Publisher · View at Google Scholar · View at Scopus
  20. M. A. Davare and J. W. Hell, “Increased phosphorylation of the neuronal L-type Ca2+ channel Cav1.2 during aging,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 26, pp. 16018–16023, 2003. View at Publisher · View at Google Scholar · View at Scopus
  21. D. D. Hall, J. A. Feekes, A. S. Arachchige Don et al., “Binding of protein phosphatase 2A to the L-type calcium channel Ca v1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation,” Biochemistry, vol. 45, no. 10, pp. 3448–3459, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. M. Bünemann, B. L. Gerhardstein, T. Gao, and M. M. Hosey, “Functional regulation of L-type calcium channels via protein kinase A- mediated phosphorylation of the β2 subunit,” The Journal of Biological Chemistry, vol. 274, no. 48, pp. 33851–33854, 1999. View at Publisher · View at Google Scholar · View at Scopus
  23. A. N. Ganesan, C. Maack, D. C. Johns, A. Sidor, and B. O'Rourke, “β-Adrenergic stimulation of L-type Ca2+ channels in cardiac myocytes requires the distal carboxyl terminus of α1C but not serine 1928,” Circulation Research, vol. 98, no. 2, pp. e11–e18, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. L. Yang, G. Liu, S. I. Zakharov et al., “Ser1928 is a common site for Cav1.2 phosphorylation by protein kinase C isoforms,” The Journal of Biological Chemistry, vol. 280, no. 1, pp. 207–214, 2005. View at Publisher · View at Google Scholar · View at Scopus
  25. T. Lemke, A. Welling, C. J. Christel et al., “Unchanged β-adrenergic stimulation of cardiac L-type calcium channels in Cav1.2 phosphorylation site S1928A mutant mice,” The Journal of Biological Chemistry, vol. 283, no. 50, pp. 34738–34744, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. V. Cena, G. P. Nicolas, P. Sanchez Garcia, S. M. Kirpekar, and A. G. Garcia, “Pharmacological dissection of receptor-associated and voltage-sensitive ionic channels involved in catecholamine release,” Neuroscience, vol. 10, no. 4, pp. 1455–1462, 1983. View at Publisher · View at Google Scholar · View at Scopus
  27. B. Avidor, T. Avidor, L. Schwartz, K. S. De Jongh, and D. Atlas, “Cardiac L-type Ca2+ channel triggers transmitter release in PC12 cells,” FEBS Letters, vol. 342, no. 2, pp. 209–213, 1994. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Hagalili, N. Bachnoff, and D. Atlas, “The Voltage-gated Ca2+ channel is the Ca2+ sensor protein of secretion,” Biochemistry, vol. 47, no. 52, pp. 13822–13830, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. O. Wiser, M. K. Bennett, and D. Atlas, “Functional interaction of syntaxin and SNAP-25 with voltage-sensitive L- and N-type Ca2+ channels,” EMBO Journal, vol. 15, no. 16, pp. 4100–4110, 1996. View at Google Scholar · View at Scopus
  30. O. Wiser, M. Trus, A. Hernández et al., “The voltage sensitive Lc-type Ca2+ channel is functionally coupled to the exocytotic machinery,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 1, pp. 248–253, 1999. View at Google Scholar · View at Scopus
  31. M. Trus, R. F. Corkey, R. Nesher et al., “The L-type voltage-gated Ca2+ channel is the Ca2+ sensor protein of stimulus-secretion coupling in pancreatic beta cells,” Biochemistry, vol. 46, no. 50, pp. 14461–14467, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. D. Atlas, “Functional and physical coupling of voltage-sensitive calcium channels with exocytotic proteins: ramifications for the secretion mechanism,” Journal of Neurochemistry, vol. 77, no. 4, pp. 972–985, 2001. View at Publisher · View at Google Scholar · View at Scopus
  33. R. Cohen, B. M. Schmitt, and D. Atlas, “Molecular identification and reconstitution of depolarization-induced exocytosis monitored by membrane capacitance,” Biophysical Journal, vol. 89, no. 6, pp. 4364–4373, 2005. View at Publisher · View at Google Scholar · View at Scopus
  34. I. Lerner, M. Trus, R. Cohen, O. Yizhar, I. Nussinovitch, and D. Atlas, “Ion interaction at the pore of Lc-type Ca2+ channel is sufficient to mediate depolarization-induced exocytosis,” Journal of Neurochemistry, vol. 97, no. 1, pp. 116–127, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. R. Cohen, B. M. Schmitt, and D. Atlas, “Reconstitution of depolarization and Ca2+-evoked secretion in xenopus oocytes monitored by membrane capacitance,” Methods in Molecular Biology, vol. 440, pp. 269–282, 2008. View at Publisher · View at Google Scholar · View at Scopus
  36. R. H. Chow, L. Von Ruden, and E. Neher, “Delay in vesicle fusion revealed by electrochemical monitoring of single secretory events in adrenal chromaffin cells,” Nature, vol. 356, no. 6364, pp. 60–63, 1992. View at Publisher · View at Google Scholar · View at Scopus
  37. U. Ashery, A. Betz, X. Tao, N. Brose, and J. Rettig, “An efficient method for infection of adrenal chromaffin cells using the Semliki Forest virus gene expression system,” European Journal of Cell Biology, vol. 78, no. 8, pp. 525–532, 1999. View at Google Scholar · View at Scopus
  38. R. M. Wightman, J. A. Jankowski, R. T. Kennedy et al., “Temporally resolved catecholamine spikes correspond to single vesicle release from individual chromaffin cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 23, pp. 10754–10758, 1991. View at Google Scholar · View at Scopus
  39. M. He, I. Bodi, G. Mikala, and A. Schwartz, “Motif III S5 of L-type calcium channels is involved in the dihydropyridine binding site. A combined radioligand binding and electrophysiological study,” The Journal of Biological Chemistry, vol. 272, no. 5, pp. 2629–2633, 1997. View at Publisher · View at Google Scholar · View at Scopus
  40. T. L. Colliver, E. J. Hess, E. N. Pothos, D. Sulzer, and A. G. Ewing, “Quantitative and statistical analysis of the shape of amperometric spikes recorded from two populations of cells,” Journal of Neurochemistry, vol. 74, no. 3, pp. 1086–1097, 2000. View at Google Scholar · View at Scopus
  41. C. T. Wang, R. Grishanin, C. A. Earles et al., “Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles,” Science, vol. 294, no. 5544, pp. 1111–1115, 2001. View at Publisher · View at Google Scholar · View at Scopus
  42. A. Yatani, J. Codina, Y. Imoto, J. Reeves, L. Birnbaumer, and A. M. Brown, “A G protein directly regulates mammalian cardiac calcium channels,” Science, vol. 238, no. 4831, pp. 1288–1292, 1987. View at Google Scholar · View at Scopus
  43. H. C. Hartzell, P. F. Mery, R. Fischmeister, and G. Szabo, “Sympathetic regulation of cardiac calcium current is due exclusively to cAMP-dependent phosphorylation,” Nature, vol. 351, no. 6327, pp. 573–576, 1991. View at Publisher · View at Google Scholar · View at Scopus
  44. H. Haase, J. Alvarez, D. Petzhold et al., “Ahnak is critical for cardiac Ca(v)1.2 calcium channel function and its β-adrenergic regulation,” FASEB Journal, vol. 19, no. 14, pp. 1969–1977, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. D. Singer-Lahat, I. Lotan, M. Biel, V. Flockerzi, F. Hofmann, and N. Dascal, “Cardiac calcium channels expressed in xenopus oocytes are modulated by dephosphorylation but not by cAMP-Dependent phosphorylation,” Receptors and Channels, vol. 2, no. 3, pp. 215–226, 1994. View at Google Scholar · View at Scopus