메뉴 건너뛰기




Volumn 103, Issue 4, 2007, Pages 347-353

Regulation of Cav1.2 current: Interaction with intracellular molecules

Author keywords

Cav1.2; Calcium; Channel; Current

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; CALCIUM CHANNEL L TYPE; CALMODULIN; CAVEOLIN 3; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PDZ PROTEIN; PHOSPHATASE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; SNARE PROTEIN; SORCIN; SYNAPTOTAGMIN; CA2+ BINDING PROTEIN 1; CA2+-BINDING PROTEIN-1; L TYPE CALCIUM CHANNEL ALPHA(1C); L-TYPE CALCIUM CHANNEL ALPHA(1C); UNCLASSIFIED DRUG;

EID: 34247385160     PISSN: 13478613     EISSN: 13478648     Source Type: Journal    
DOI: 10.1254/jphs.CR0070012     Document Type: Review
Times cited : (33)

References (55)
  • 1
    • 0029134828 scopus 로고
    • Molecular biology of calcium channels
    • Perez-Reyes E, Schneider T. Molecular biology of calcium channels. Kidney Int. 1995;48:1111-1124.
    • (1995) Kidney Int , vol.48 , pp. 1111-1124
    • Perez-Reyes, E.1    Schneider, T.2
  • 3
    • 8644255945 scopus 로고    scopus 로고
    • Calmodulin reverses rundown of L-type Ca(2+) channels in guinea pig ventricular myocytes
    • Xu JJ, Hao LY, Kameyama A, Kameyama M. Calmodulin reverses rundown of L-type Ca(2+) channels in guinea pig ventricular myocytes. Am J Physiol Cell Physiol. 2004;287:C1717-C1724.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Xu, J.J.1    Hao, L.Y.2    Kameyama, A.3    Kameyama, M.4
  • 4
    • 0035903175 scopus 로고    scopus 로고
    • Molecular basis of calmodulin tethering and Ca2+- dependent inactivation of L-type Ca2+ channels
    • Pitt GS, Zuhlke RD, Hudmon A, Schulman H, Reuter H, Tsien RW. Molecular basis of calmodulin tethering and Ca2+- dependent inactivation of L-type Ca2+ channels. J Biol Chem. 2001;276:30794-30802.
    • (2001) J Biol Chem , vol.276 , pp. 30794-30802
    • Pitt, G.S.1    Zuhlke, R.D.2    Hudmon, A.3    Schulman, H.4    Reuter, H.5    Tsien, R.W.6
  • 5
    • 0037629688 scopus 로고    scopus 로고
    • FRET two-hybrid mapping reveals function and location of L-type Ca2+ channel CaM preassociation
    • Erickson MG, Liang H, Mori MX, Yue DT. FRET two-hybrid mapping reveals function and location of L-type Ca2+ channel CaM preassociation. Neuron. 2003;39:97-107.
    • (2003) Neuron , vol.39 , pp. 97-107
    • Erickson, M.G.1    Liang, H.2    Mori, M.X.3    Yue, D.T.4
  • 6
    • 1942488175 scopus 로고    scopus 로고
    • Functional stoichiometry and local enrichment of calmodulin interacting with Ca2+ channels
    • Mori MX, Erickson MG, Yue DT. Functional stoichiometry and local enrichment of calmodulin interacting with Ca2+ channels. Science. 2004;304:432-435.
    • (2004) Science , vol.304 , pp. 432-435
    • Mori, M.X.1    Erickson, M.G.2    Yue, D.T.3
  • 7
    • 28544446450 scopus 로고    scopus 로고
    • Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex
    • Van Petegem F, Chatelain FC, Minor DL Jr. Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex. Nat Struct Mol Biol. 2005;12:1108-1115.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1108-1115
    • Van Petegem, F.1    Chatelain, F.C.2    Minor Jr., D.L.3
  • 8
    • 23844535091 scopus 로고    scopus 로고
    • Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1
    • Zhou H, Yu K, McCoy KL, Lee A. Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1. J Biol Chem. 2005;280:29612-29619.
    • (2005) J Biol Chem , vol.280 , pp. 29612-29619
    • Zhou, H.1    Yu, K.2    McCoy, K.L.3    Lee, A.4
  • 10
    • 0036890075 scopus 로고    scopus 로고
    • Differential transcriptional expression of Ca2+ BP superfamilies in murine gastrointestinal smooth muscles
    • Ohya S, Horowitz B. Differential transcriptional expression of Ca2+ BP superfamilies in murine gastrointestinal smooth muscles. Am J Physiol Gastrointest Liver Physiol. 2002;283:G1290-G1297.
    • (2002) Am J Physiol Gastrointest Liver Physiol , vol.283
    • Ohya, S.1    Horowitz, B.2
  • 11
    • 2442684236 scopus 로고    scopus 로고
    • Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels
    • Zhou H, Kim SA, Kirk EA, Tippens AL, Sun H, Haeseleer F, et al. Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels. J Neurosci. 2004;24:4698-4708.
    • (2004) J Neurosci , vol.24 , pp. 4698-4708
    • Zhou, H.1    Kim, S.A.2    Kirk, E.A.3    Tippens, A.L.4    Sun, H.5    Haeseleer, F.6
  • 12
    • 27744483468 scopus 로고    scopus 로고
    • CaMKII tethers to L-type Ca2+ channels, establishing a local and dedicated integrator of Ca2+ signals for facilitation
    • Hudmon A, Schulman H, Kim J, Maltez JM, Tsien RW, Pitt GS. CaMKII tethers to L-type Ca2+ channels, establishing a local and dedicated integrator of Ca2+ signals for facilitation. J Cell Biol. 2005;171:537-547.
    • (2005) J Cell Biol , vol.171 , pp. 537-547
    • Hudmon, A.1    Schulman, H.2    Kim, J.3    Maltez, J.M.4    Tsien, R.W.5    Pitt, G.S.6
  • 13
    • 33747881612 scopus 로고    scopus 로고
    • L-type Ca2+ channel facilitation mediated by phosphorylation of the beta subunit by CaMKII
    • Grueter CE, Abiria SA, Dzhura I, Wu Y, Ham AJ, Mohler PJ, et al. L-type Ca2+ channel facilitation mediated by phosphorylation of the beta subunit by CaMKII. Mol Cell. 2006;23:641-650.
    • (2006) Mol Cell , vol.23 , pp. 641-650
    • Grueter, C.E.1    Abiria, S.A.2    Dzhura, I.3    Wu, Y.4    Ham, A.J.5    Mohler, P.J.6
  • 14
    • 33748741562 scopus 로고    scopus 로고
    • Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: Identification of the phosphorylation sites
    • Lee TS, Karl R, Moosmang S, Lenhardt P, Klugbauer N, Hofmann F, et al. Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: Identification of the phosphorylation sites. J Biol Chem. 2006;281:25560-25567.
    • (2006) J Biol Chem , vol.281 , pp. 25560-25567
    • Lee, T.S.1    Karl, R.2    Moosmang, S.3    Lenhardt, P.4    Klugbauer, N.5    Hofmann, F.6
  • 15
    • 3242716356 scopus 로고    scopus 로고
    • A-kinase anchoring protein targeting of protein kinase A in the heart
    • Ruehr ML, Russell MA, Bond M. A-kinase anchoring protein targeting of protein kinase A in the heart. J Mol Cell Cardiol. 2004;37:653-665.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 653-665
    • Ruehr, M.L.1    Russell, M.A.2    Bond, M.3
  • 16
    • 0032078084 scopus 로고    scopus 로고
    • Primary structure and function of an A kinase anchoring protein associated with calcium channels
    • Gray PC, Johnson BD, Westenbroek RE, Hays LG, Yates JR 3rd, Scheuer T, et al. Primary structure and function of an A kinase anchoring protein associated with calcium channels. Neuron. 1998;20:1017-1026.
    • (1998) Neuron , vol.20 , pp. 1017-1026
    • Gray, P.C.1    Johnson, B.D.2    Westenbroek, R.E.3    Hays, L.G.4    Yates 3rd, J.R.5    Scheuer, T.6
  • 17
    • 2642705036 scopus 로고    scopus 로고
    • A novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane events
    • Fraser ID, Tavalin SJ, Lester LB, Langeberg LK, Westphal AM, Dean RA, et al. A novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane events. EMBO J. 1998;17:2261-2272.
    • (1998) EMBO J , vol.17 , pp. 2261-2272
    • Fraser, I.D.1    Tavalin, S.J.2    Lester, L.B.3    Langeberg, L.K.4    Westphal, A.M.5    Dean, R.A.6
  • 18
    • 0242331601 scopus 로고    scopus 로고
    • Beta-adrenergic regulation requires direct anchoring of PKA to cardiac CaV1.2 channels via a leucine zipper interaction with A kinase-anchoring protein 15
    • Hulme JT, Lin TW, Westenbroek RE, Scheuer T, Catterall WA. Beta-adrenergic regulation requires direct anchoring of PKA to cardiac CaV1.2 channels via a leucine zipper interaction with A kinase-anchoring protein 15. Proc Natl Acad Sci U S A. 2003;100:13093-13098.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13093-13098
    • Hulme, J.T.1    Lin, T.W.2    Westenbroek, R.E.3    Scheuer, T.4    Catterall, W.A.5
  • 19
    • 0033569750 scopus 로고    scopus 로고
    • The A-kinase anchor protein MAP2B and cAMP-dependent protein kinase are associated with class C L-type calcium channels in neurons
    • Davare MA, Dong F, Rubin CS, Hell JW. The A-kinase anchor protein MAP2B and cAMP-dependent protein kinase are associated with class C L-type calcium channels in neurons. J Biol Chem. 1999;274:30280-30287.
    • (1999) J Biol Chem , vol.274 , pp. 30280-30287
    • Davare, M.A.1    Dong, F.2    Rubin, C.S.3    Hell, J.W.4
  • 20
    • 0034671738 scopus 로고    scopus 로고
    • Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase
    • Davare MA, Horne MC, Hell JW. Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase. J Biol Chem. 2000;275:39710-39717.
    • (2000) J Biol Chem , vol.275 , pp. 39710-39717
    • Davare, M.A.1    Horne, M.C.2    Hell, J.W.3
  • 21
    • 33644849005 scopus 로고    scopus 로고
    • Binding of protein phosphatase 2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation
    • Hall DD, Feekes JA, Arachchige Don AS, Shi M, Hamid J, Chen L, et al. Binding of protein phosphatase 2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation. Biochemistry. 2006;45:3448-3459.
    • (2006) Biochemistry , vol.45 , pp. 3448-3459
    • Hall, D.D.1    Feekes, J.A.2    Arachchige Don, A.S.3    Shi, M.4    Hamid, J.5    Chen, L.6
  • 22
    • 0030016356 scopus 로고    scopus 로고
    • Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes
    • duBell WH, Lederer WJ, Rogers TB. Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes. J Physiol. 1996;493:793-800.
    • (1996) J Physiol , vol.493 , pp. 793-800
    • duBell, W.H.1    Lederer, W.J.2    Rogers, T.B.3
  • 23
    • 1942517938 scopus 로고    scopus 로고
    • Protein phosphatase 1 and an opposing protein kinase regulate steady-state L-type Ca2+ current in mouse cardiac myocytes
    • duBell WH, Rogers TB. Protein phosphatase 1 and an opposing protein kinase regulate steady-state L-type Ca2+ current in mouse cardiac myocytes. J Physiol. 2004;556:79-93.
    • (2004) J Physiol , vol.556 , pp. 79-93
    • duBell, W.H.1    Rogers, T.B.2
  • 24
    • 0030611692 scopus 로고    scopus 로고
    • Intracellular Ca2+ inhibits smooth muscle L-type Ca2+ channels by activation of protein phosphatase type 2B and by direct interaction with the channel
    • Schuhmann K, Romanin C, Baumgartner W, Groschner K. Intracellular Ca2+ inhibits smooth muscle L-type Ca2+ channels by activation of protein phosphatase type 2B and by direct interaction with the channel. J Gen Physiol. 1997;110:503-513.
    • (1997) J Gen Physiol , vol.110 , pp. 503-513
    • Schuhmann, K.1    Romanin, C.2    Baumgartner, W.3    Groschner, K.4
  • 25
    • 0030933022 scopus 로고    scopus 로고
    • Mechanism of Ca(2+)-dependent inactivation of L-type Ca2+ channels in GH3 cells: Direct evidence against dephosphorylation by calcineurin
    • Victor RG, Rusnak F, Sikkink R, Marban E, O'Rourke B. Mechanism of Ca(2+)-dependent inactivation of L-type Ca2+ channels in GH3 cells: direct evidence against dephosphorylation by calcineurin. J Membr Biol. 1997;156:53-61.
    • (1997) J Membr Biol , vol.156 , pp. 53-61
    • Victor, R.G.1    Rusnak, F.2    Sikkink, R.3    Marban, E.4    O'Rourke, B.5
  • 26
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: From cell biology to animal physiology
    • Razani B, Woodman SE, Lisanti MP. Caveolae: from cell biology to animal physiology. Pharmacol Rev. 2002;54:431-467.
    • (2002) Pharmacol Rev , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 27
    • 0030060941 scopus 로고    scopus 로고
    • Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle
    • Tang Z, Scherer PE, Okamoto T, Song K, Chu C, Kohtz DS, et al. Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem. 1996;271:2255-2261.
    • (1996) J Biol Chem , vol.271 , pp. 2255-2261
    • Tang, Z.1    Scherer, P.E.2    Okamoto, T.3    Song, K.4    Chu, C.5    Kohtz, D.S.6
  • 28
    • 33646592211 scopus 로고    scopus 로고
    • Localization of cardiac L-type Ca(2+) channels to a caveolar macromolecular signaling complex is required for beta(2)-adrenergic regulation
    • Balijepalli RC, Foell JD, Hall DD, Hell JW, Kamp TJ. Localization of cardiac L-type Ca(2+) channels to a caveolar macromolecular signaling complex is required for beta(2)-adrenergic regulation. Proc Natl Acad Sci U S A. 2006;103:7500-7505.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7500-7505
    • Balijepalli, R.C.1    Foell, J.D.2    Hall, D.D.3    Hell, J.W.4    Kamp, T.J.5
  • 29
    • 0035816616 scopus 로고    scopus 로고
    • A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2
    • Davare MA, Avdonin V, Hall DD, Peden EM, Burette A, Weinberg RJ, et al. A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2. Science. 2001;293:98-101.
    • (2001) Science , vol.293 , pp. 98-101
    • Davare, M.A.1    Avdonin, V.2    Hall, D.D.3    Peden, E.M.4    Burette, A.5    Weinberg, R.J.6
  • 30
    • 0038076070 scopus 로고    scopus 로고
    • Interactions with PDZ proteins are required for L-type calcium channels to activate cAMP response element-binding protein-dependent gene expression
    • Weick JP, Groth RD, Isaksen AL, Mermelstein PG. Interactions with PDZ proteins are required for L-type calcium channels to activate cAMP response element-binding protein-dependent gene expression. J Neurosci. 2003;23:3446-3456.
    • (2003) J Neurosci , vol.23 , pp. 3446-3456
    • Weick, J.P.1    Groth, R.D.2    Isaksen, A.L.3    Mermelstein, P.G.4
  • 31
    • 13944250584 scopus 로고    scopus 로고
    • Association of CaV1.3 L-type calcium channels with Shank
    • Zhang H, Maximov A, Fu Y, Xu F, Tang TS, Tkatch T, et al. Association of CaV1.3 L-type calcium channels with Shank. J Neurosci. 2005;25:1037-1049.
    • (2005) J Neurosci , vol.25 , pp. 1037-1049
    • Zhang, H.1    Maximov, A.2    Fu, Y.3    Xu, F.4    Tang, T.S.5    Tkatch, T.6
  • 32
    • 0033568846 scopus 로고    scopus 로고
    • Neuronal interleukin-16 (NIL-16): A dual function PDZ domain protein
    • Kurschner C, Yuzaki M. Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein. J Neurosci. 1999;19:7770-7780.
    • (1999) J Neurosci , vol.19 , pp. 7770-7780
    • Kurschner, C.1    Yuzaki, M.2
  • 34
    • 0032563129 scopus 로고    scopus 로고
    • Sorcin associates with the pore-forming subunit of voltage-dependent L-type Ca2+ channels
    • Meyers MB, Puri TS, Chien AJ, Gao T, Hsu PH, Hosey MM, et al. Sorcin associates with the pore-forming subunit of voltage-dependent L-type Ca2+ channels. J Biol Chem. 1998;273:18930-18935.
    • (1998) J Biol Chem , vol.273 , pp. 18930-18935
    • Meyers, M.B.1    Puri, T.S.2    Chien, A.J.3    Gao, T.4    Hsu, P.H.5    Hosey, M.M.6
  • 36
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 1998;395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 37
    • 0037630703 scopus 로고    scopus 로고
    • Regulation of presynaptic calcium channels by synaptic proteins
    • Zamponi GW. Regulation of presynaptic calcium channels by synaptic proteins. J Pharmacol Sci. 2003;92:79-83.
    • (2003) J Pharmacol Sci , vol.92 , pp. 79-83
    • Zamponi, G.W.1
  • 38
    • 9144243918 scopus 로고    scopus 로고
    • The synaptotagmins: Calcium sensors for vesicular trafficking
    • Yoshihara M, Montana ES. The synaptotagmins: calcium sensors for vesicular trafficking. Neuroscientist. 2004;10:566-574.
    • (2004) Neuroscientist , vol.10 , pp. 566-574
    • Yoshihara, M.1    Montana, E.S.2
  • 39
    • 0033524419 scopus 로고    scopus 로고
    • The voltage sensitive Lc-type Ca2+ channel is functionally coupled to the exocytotic machinery
    • Wiser O, Trus M, Hernandez A, Renstrom E, Barg S, Rorsman P, et al. The voltage sensitive Lc-type Ca2+ channel is functionally coupled to the exocytotic machinery. Proc Natl Acad Sci U S A. 1999;96:248-253.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 248-253
    • Wiser, O.1    Trus, M.2    Hernandez, A.3    Renstrom, E.4    Barg, S.5    Rorsman, P.6
  • 40
    • 0038321954 scopus 로고    scopus 로고
    • The C2A domain of synaptotagmin alters the kinetics of voltage-gated Ca2+ channels Ca(v)1.2 (Lc-type) and Ca(v)2.3 (R-type)
    • Cohen R, Elferink LA, Atlas D. The C2A domain of synaptotagmin alters the kinetics of voltage-gated Ca2+ channels Ca(v)1.2 (Lc-type) and Ca(v)2.3 (R-type). J Biol Chem. 2003;278:9258-9266.
    • (2003) J Biol Chem , vol.278 , pp. 9258-9266
    • Cohen, R.1    Elferink, L.A.2    Atlas, D.3
  • 41
    • 24044497631 scopus 로고    scopus 로고
    • Direct interaction between SNAP-23 and L-type Ca2+ channel
    • Cho WJ, Jeremic A, Jena BP. Direct interaction between SNAP-23 and L-type Ca2+ channel. J Cell Mol Med. 2005;9:380-386.
    • (2005) J Cell Mol Med , vol.9 , pp. 380-386
    • Cho, W.J.1    Jeremic, A.2    Jena, B.P.3
  • 42
    • 33644824170 scopus 로고    scopus 로고
    • Alternative splicing of the voltage-gated Ca2+ channel beta4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex
    • Vendel AC, Terry MD, Striegel AR, Iverson NM, Leuranguer V, Rithner CD, et al. Alternative splicing of the voltage-gated Ca2+ channel beta4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex. J Neurosci. 2006;26:2635-2644.
    • (2006) J Neurosci , vol.26 , pp. 2635-2644
    • Vendel, A.C.1    Terry, M.D.2    Striegel, A.R.3    Iverson, N.M.4    Leuranguer, V.5    Rithner, C.D.6
  • 43
    • 0035098524 scopus 로고    scopus 로고
    • JAB1/CSN5 and the COP9 signalosome. A complex situation
    • 2:96-101
    • Chamovitz DA, Segal D. JAB1/CSN5 and the COP9 signalosome. A complex situation. EMBO Rep. 2001;2:96-101.
    • EMBO Rep. 2001
    • Chamovitz, D.A.1    Segal, D.2
  • 44
    • 33645055408 scopus 로고    scopus 로고
    • CSN5/ Jab1 inhibits cardiac L-type Ca2+ channel activity through protein-protein interactions
    • Kameda K, Fukao M, Kobayashi T, Tsutsuura M, Nagashima M, Yamada Y, et al. CSN5/ Jab1 inhibits cardiac L-type Ca2+ channel activity through protein-protein interactions. J Mol Cell Cardiol. 2006;40:562-569.
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 562-569
    • Kameda, K.1    Fukao, M.2    Kobayashi, T.3    Tsutsuura, M.4    Nagashima, M.5    Yamada, Y.6
  • 45
    • 0345060805 scopus 로고    scopus 로고
    • Regulation of voltage-gated calcium channel activity by the Rem and Rad GTPases
    • Finlin BS, Crump SM, Satin J, Andres DA. Regulation of voltage-gated calcium channel activity by the Rem and Rad GTPases. Proc Natl Acad Sci U S A. 2003;100:14469-14474.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14469-14474
    • Finlin, B.S.1    Crump, S.M.2    Satin, J.3    Andres, D.A.4
  • 46
    • 23944515401 scopus 로고    scopus 로고
    • Regulation of L-type Ca2+ channel activity and insulin secretion by the Rem2 GTPase
    • Finlin BS, Mosley AL, Crump SM, Correll RN, Ozcan S, Satin J, et al. Regulation of L-type Ca2+ channel activity and insulin secretion by the Rem2 GTPase. J Biol Chem. 2005;280:41864-41871.
    • (2005) J Biol Chem , vol.280 , pp. 41864-41871
    • Finlin, B.S.1    Mosley, A.L.2    Crump, S.M.3    Correll, R.N.4    Ozcan, S.5    Satin, J.6
  • 48
    • 0035821585 scopus 로고    scopus 로고
    • Regulation of Ca2+ channel expression at the cell surface by the small G-protein kir/Gem
    • Beguin P, Nagashima K, Gonoi T, Shibasaki T, Takahashi K, Kashima Y, et al. Regulation of Ca2+ channel expression at the cell surface by the small G-protein kir/Gem. Nature. 2001;411:701-706.
    • (2001) Nature , vol.411 , pp. 701-706
    • Beguin, P.1    Nagashima, K.2    Gonoi, T.3    Shibasaki, T.4    Takahashi, K.5    Kashima, Y.6
  • 49
    • 33749323918 scopus 로고    scopus 로고
    • Crump SM, Correll RN, Schroder EA, Lester WC, Finlin BS, Andres DA, et al. L-type calcium channel {alpha}-subunit and protein kinase inhibitors modulate Rem-mediated regulation of current. Am J Physiol Heart Circ Physiol. 2006;291:H1959-H1971.
    • Crump SM, Correll RN, Schroder EA, Lester WC, Finlin BS, Andres DA, et al. L-type calcium channel {alpha}-subunit and protein kinase inhibitors modulate Rem-mediated regulation of current. Am J Physiol Heart Circ Physiol. 2006;291:H1959-H1971.
  • 50
  • 51
    • 23944467523 scopus 로고    scopus 로고
    • Roles of 14-3-3 and calmodulin binding in subcellular localization and function of the small Gprotein Rem2
    • Beguin P, Mahalakshmi RN, Nagashima K, Cher DH, Kuwamura N, Yamada Y, et al. Roles of 14-3-3 and calmodulin binding in subcellular localization and function of the small Gprotein Rem2. Biochem J. 2005;390:67-75.
    • (2005) Biochem J , vol.390 , pp. 67-75
    • Beguin, P.1    Mahalakshmi, R.N.2    Nagashima, K.3    Cher, D.H.4    Kuwamura, N.5    Yamada, Y.6
  • 52
    • 0032765048 scopus 로고    scopus 로고
    • Signaling from beta-adrenoceptor to L-type calcium channel: Identification of a novel cardiac protein kinase A target possessing similarities to AHNAK
    • Haase H, Podzuweit T, Lutsch G, Hohaus A, Kostka S, Lindschau C, et al. Signaling from beta-adrenoceptor to L-type calcium channel: identification of a novel cardiac protein kinase A target possessing similarities to AHNAK. FASEB J. 1999;13:2161-2172.
    • (1999) FASEB J , vol.13 , pp. 2161-2172
    • Haase, H.1    Podzuweit, T.2    Lutsch, G.3    Hohaus, A.4    Kostka, S.5    Lindschau, C.6
  • 53
    • 0036325857 scopus 로고    scopus 로고
    • The carboxyl-terminal region of ahnak provides a link between cardiac L-type Ca2+ channels and the actin-based cytoskeleton
    • Hohaus A, Person V, Behlke J, Schaper J, Morano I, Haase H. The carboxyl-terminal region of ahnak provides a link between cardiac L-type Ca2+ channels and the actin-based cytoskeleton. FASEB J. 2002;16:1205-1216.
    • (2002) FASEB J , vol.16 , pp. 1205-1216
    • Hohaus, A.1    Person, V.2    Behlke, J.3    Schaper, J.4    Morano, I.5    Haase, H.6
  • 54
    • 28744458169 scopus 로고    scopus 로고
    • Ahnak is critical for cardiac Ca(V)1.2 calcium channel function and its beta-adrenergic regulation
    • Haase H, Alvarez J, Petzhold D, Doller A, Behlke J, Erdmann J, et al. Ahnak is critical for cardiac Ca(V)1.2 calcium channel function and its beta-adrenergic regulation. FASEB J. 2005;19:1969-1977.
    • (2005) FASEB J , vol.19 , pp. 1969-1977
    • Haase, H.1    Alvarez, J.2    Petzhold, D.3    Doller, A.4    Behlke, J.5    Erdmann, J.6
  • 55
    • 23744438810 scopus 로고    scopus 로고
    • Calcium signaling in cardiac ventricular myocytes
    • Bers DM, Guo T. Calcium signaling in cardiac ventricular myocytes. Ann N Y Acad Sci. 2005;1047:86-98.
    • (2005) Ann N Y Acad Sci , vol.1047 , pp. 86-98
    • Bers, D.M.1    Guo, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.