메뉴 건너뛰기




Volumn 202, Issue 3, 2013, Pages 453-462

The inner and outer compartments of mitochondria are sites of distinct cAMP/PKA signaling dynamics

Author keywords

[No Author keywords available]

Indexed keywords

BICARBONATE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHATASE;

EID: 84884227999     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201303159     Document Type: Article
Times cited : (122)

References (44)
  • 1
    • 77953567491 scopus 로고    scopus 로고
    • Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects
    • Acin-Perez, R., E. Salazar, S. Brosel, H. Yang, E.A. Schon, and G. Manfredi. 2009a. Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects. EMBO Mol Med. 1:392-406. http://dx.doi.org/10.1002/emmm.200900046
    • (2009) EMBO Mol Med. , vol.1 , pp. 392-406
    • Acin-Perez, R.1    Salazar, E.2    Brosel, S.3    Yang, H.4    Schon, E.A.5    Manfredi, G.6
  • 2
    • 60649095658 scopus 로고    scopus 로고
    • Cyclic AMP produced inside mitochondria regulates oxidative phosphorylation
    • Acin-Perez, R., E. Salazar, M. Kamenetsky, J. Buck, L.R. Levin, and G. Manfredi. 2009b. Cyclic AMP produced inside mitochondria regulates oxidative phosphorylation. Cell Metab. 9:265-276. http://dx.doi.org/10.1016/j.cmet.2009.01.012
    • (2009) Cell Metab. , vol.9 , pp. 265-276
    • Acin-Perez, R.1    Salazar, E.2    Kamenetsky, M.3    Buck, J.4    Levin, L.R.5    Manfredi, G.6
  • 3
    • 79958034385 scopus 로고    scopus 로고
    • Protein phosphorylation and prevention of cytochrome oxidase inhibition by ATP: coupled mechanisms of energy metabolism regulation
    • Acin-Perez, R., D.L. Gatti, Y. Bai, and G. Manfredi. 2011a. Protein phosphorylation and prevention of cytochrome oxidase inhibition by ATP: coupled mechanisms of energy metabolism regulation. Cell Metab. 13:712-719. http://dx.doi.org/10.1016/j.cmet.2011.03.024
    • (2011) Cell Metab. , vol.13 , pp. 712-719
    • Acin-Perez, R.1    Gatti, D.L.2    Bai, Y.3    Manfredi, G.4
  • 5
    • 77951682590 scopus 로고    scopus 로고
    • Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity
    • Agnes, R.S., F. Jernigan, J.R. Shell, V. Sharma, and D.S. Lawrence. 2010. Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity. J. Am. Chem. Soc. 132:6075-6080. http://dx.doi.org/10.1021/ja909652q
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6075-6080
    • Agnes, R.S.1    Jernigan, F.2    Shell, J.R.3    Sharma, V.4    Lawrence, D.S.5
  • 6
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • Allen, M.D., and J. Zhang. 2006. Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters. Biochem. Biophys. Res. Commun. 348:716-721. http://dx.doi.org/10.1016/j.bbrc.2006.07.136
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 8
    • 0033965893 scopus 로고    scopus 로고
    • The allosteric ATP-inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP-dependent phosphorylation
    • Bender, E., and B. Kadenbach. 2000. The allosteric ATP-inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP-dependent phosphorylation. FEBS Lett. 466:130-134. http://dx.doi.org/10.1016/S0014-5793(99)01773-1
    • (2000) FEBS Lett. , vol.466 , pp. 130-134
    • Bender, E.1    Kadenbach, B.2
  • 10
    • 56349110884 scopus 로고    scopus 로고
    • Control of mitochondria dynamics and oxidative metabolism by cAMP, AKAPs and the proteasome
    • Carlucci, A., L. Lignitto, and A. Feliciello. 2008. Control of mitochondria dynamics and oxidative metabolism by cAMP, AKAPs and the proteasome. Trends Cell Biol. 18:604-613. http://dx.doi.org/10.1016/j.tcb.2008.09.006
    • (2008) Trends Cell Biol. , vol.18 , pp. 604-613
    • Carlucci, A.1    Lignitto, L.2    Feliciello, A.3
  • 11
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang, C.-R., and C. Blackstone. 2007. Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 282:21583-21587. http://dx.doi.org/10.1074/jbc.C700083200
    • (2007) J. Biol. Chem. , vol.282 , pp. 21583-21587
    • Chang, C.-R.1    Blackstone, C.2
  • 12
    • 84867733931 scopus 로고    scopus 로고
    • Cardiac mitochondrial matrix and respiratory complex protein phosphorylation
    • Covian, R., and R.S. Balaban. 2012. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation. Am. J. Physiol. Heart Circ. Physiol. 303:H940-H966. http://dx.doi.org/10.1152/ajpheart.00077.2012
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.303
    • Covian, R.1    Balaban, R.S.2
  • 13
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs, J.T., and S. Strack. 2007. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8:939-944. http://dx.doi.org/10.1038/sj.embor.7401062
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 14
    • 77954301751 scopus 로고    scopus 로고
    • Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
    • Csordás, G., P. Várnai, T. Golenár, S. Roy, G. Purkins, T.G. Schneider, T. Balla, and G. Hajnóczky. 2010. Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol. Cell. 39:121-132. http://dx.doi.org/10.1016/j.molcel.2010.06.029
    • (2010) Mol. Cell. , vol.39 , pp. 121-132
    • Csordás, G.1    Várnai, P.2    Golenár, T.3    Roy, S.4    Purkins, G.5    Schneider, T.G.6    Balla, T.7    Hajnóczky, G.8
  • 15
    • 78951493639 scopus 로고    scopus 로고
    • ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function
    • Darshi, M., V.L. Mendiola, M.R. Mackey, A.N. Murphy, A. Koller, G.A. Perkins, M.H. Ellisman, and S.S. Taylor. 2011. ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function. J. Biol. Chem. 286:2918-2932. http://dx.doi.org/10.1074/jbc.M110.171975
    • (2011) J. Biol. Chem. , vol.286 , pp. 2918-2932
    • Darshi, M.1    Mendiola, V.L.2    Mackey, M.R.3    Murphy, A.N.4    Koller, A.5    Perkins, G.A.6    Ellisman, M.H.7    Taylor, S.S.8
  • 17
    • 78650157273 scopus 로고    scopus 로고
    • Visualization of PKA activity in plasma membrane microdomains
    • Depry, C., M.D. Allen, and J. Zhang. 2011. Visualization of PKA activity in plasma membrane microdomains. Mol. Biosyst. 7:52-58. http://dx.doi.org/10.1039/c0mb00079e
    • (2011) Mol. Biosyst. , vol.7 , pp. 52-58
    • Depry, C.1    Allen, M.D.2    Zhang, J.3
  • 18
    • 80051936634 scopus 로고    scopus 로고
    • A fortykilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani, D., A. Raffaello, E. Teardo, I. Szabò, and R. Rizzuto. 2011. A fortykilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature. 476:336-340. http://dx.doi.org/10.1038/nature10230
    • (2011) Nature. , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabò, I.4    Rizzuto, R.5
  • 19
    • 9344220483 scopus 로고    scopus 로고
    • Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments
    • DiPilato, L.M., X. Cheng, and J. Zhang. 2004. Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments. Proc. Natl. Acad. Sci. USA. 101:16513-16518. http://dx.doi.org/10.1073/pnas.0405973101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 16513-16518
    • DiPilato, L.M.1    Cheng, X.2    Zhang, J.3
  • 20
    • 9644262531 scopus 로고    scopus 로고
    • cAMP-PKA signaling to the mitochondria: protein scaffolds, mRNA and phosphatases
    • Feliciello, A., M.E. Gottesman, and E.V. Avvedimento. 2005. cAMP-PKA signaling to the mitochondria: protein scaffolds, mRNA and phosphatases. Cell. Signal. 17:279-287. http://dx.doi.org/10.1016/j.cellsig.2004.09.009
    • (2005) Cell. Signal. , vol.17 , pp. 279-287
    • Feliciello, A.1    Gottesman, M.E.2    Avvedimento, E.V.3
  • 21
    • 10944237231 scopus 로고    scopus 로고
    • Improved strategies for the delivery of GFP-based Ca2+ sensors into the mitochondrial matrix
    • Filippin, L., M.C. Abad, S. Gastaldello, P.J. Magalhães, D. Sandonà, and T. Pozzan. 2005. Improved strategies for the delivery of GFP-based Ca2+ sensors into the mitochondrial matrix. Cell Calcium. 37:129-136. http://dx.doi.org/10.1016/j.ceca.2004.08.002
    • (2005) Cell Calcium. , vol.37 , pp. 129-136
    • Filippin, L.1    Abad, M.C.2    Gastaldello, S.3    Magalhães, P.J.4    Sandonà, D.5    Pozzan, T.6
  • 22
    • 33750523442 scopus 로고    scopus 로고
    • Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis
    • Hajnóczky, G., G. Csordás, S. Das, C. Garcia-Perez, M. Saotome, S. Sinha Roy, and M. Yi. 2006. Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis. Cell Calcium. 40:553-560. http://dx.doi.org/10.1016/j.ceca.2006.08.016
    • (2006) Cell Calcium. , vol.40 , pp. 553-560
    • Hajnóczky, G.1    Csordás, G.2    Das, S.3    Garcia-Perez, C.4    Saotome, M.5    Sinha Roy, S.6    Yi, M.7
  • 23
    • 0033120591 scopus 로고
    • Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A
    • Harada, H., B. Becknell, M. Wilm, M. Mann, L.J. Huang, S.S. Taylor, J.D. Scott, and S.J. Korsmeyer. 0999. Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A. Mol. Cell. 3:413-422. http://dx.doi.org/10.1016/S1097-2765(00)80469-4
    • (999) Mol. Cell. , vol.3 , pp. 413-422
    • Harada, H.1    Becknell, B.2    Wilm, M.3    Mann, M.4    Huang, L.J.5    Taylor, S.S.6    Scott, J.D.7    Korsmeyer, S.J.8
  • 25
    • 77951745863 scopus 로고    scopus 로고
    • Sphingosine kinase interacting protein is an A-kinase anchoring protein specific for type I cAMP-dependent protein kinase
    • Kovanich, D., M.A. van der Heyden, T.T. Aye, T.A. van Veen, A.J. Heck, and A. Scholten. 2010. Sphingosine kinase interacting protein is an A-kinase anchoring protein specific for type I cAMP-dependent protein kinase. ChemBioChem. 11:963-971. http://dx.doi.org/10.1002/cbic.201000058
    • (2010) ChemBioChem. , vol.11 , pp. 963-971
    • Kovanich, D.1    van der Heyden, M.A.2    Aye, T.T.3    van Veen, T.A.4    Heck, A.J.5    Scholten, A.6
  • 27
    • 0023696764 scopus 로고
    • Immunogold localization of the regulatory subunit of a type II cAMPdependent protein kinase tightly associated with mammalian sperm flagella
    • Lieberman, S.J., W. Wasco, J. MacLeod, P. Satir, and G.A. Orr. 0988. Immunogold localization of the regulatory subunit of a type II cAMPdependent protein kinase tightly associated with mammalian sperm flagella. J. Cell Biol. 107:1809-1816. http://dx.doi.org/10.1083/jcb.107.5.1809
    • (988) J. Cell Biol. , vol.107 , pp. 1809-1816
    • Lieberman, S.J.1    Wasco, W.2    MacLeod, J.3    Satir, P.4    Orr, G.A.5
  • 28
    • 84872271398 scopus 로고    scopus 로고
    • Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
    • Lu, B., J. Lee, X. Nie, M. Li, Y.I. Morozov, S. Venkatesh, D.F. Bogenhagen, D. Temiakov, and C.K. Suzuki. 2013. Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease. Mol. Cell. 49:121-132.
    • (2013) Mol. Cell. , vol.49 , pp. 121-132
    • Lu, B.1    Lee, J.2    Nie, X.3    Li, M.4    Morozov, Y.I.5    Venkatesh, S.6    Bogenhagen, D.F.7    Temiakov, D.8    Suzuki, C.K.9
  • 31
    • 79960486405 scopus 로고    scopus 로고
    • Ca2+ regulation of mitochondrial ATP synthesis visualized at the single cell level
    • Nakano, M., H. Imamura, T. Nagai, and H. Noji. 2011. Ca2+ regulation of mitochondrial ATP synthesis visualized at the single cell level. ACS Chem. Biol. 6:709-715. http://dx.doi.org/10.1021/cb100313n
    • (2011) ACS Chem. Biol. , vol.6 , pp. 709-715
    • Nakano, M.1    Imamura, H.2    Nagai, T.3    Noji, H.4
  • 32
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer, D.D., and S. Ferguson-Miller. 2003. Mitochondria: releasing power for life and unleashing the machineries of death. Cell. 112:481-490. http://dx.doi.org/10.1016/S0092-8674(03)00116-8
    • (2003) Cell. , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 33
    • 81955165133 scopus 로고    scopus 로고
    • Mitochondrial protein phosphorylation as a regulatory modality: implications for mitochondrial dysfunction in heart failure
    • O'Rourke, B., J.E. Van Eyk, and D.B. Foster. 2011. Mitochondrial protein phosphorylation as a regulatory modality: implications for mitochondrial dysfunction in heart failure. Congest. Heart Fail. 17:269-282. http://dx.doi.org/10.1111/j.1751-7133.2011.00266.x
    • (2011) Congest. Heart Fail. , vol.17 , pp. 269-282
    • O'Rourke, B.1    Van Eyk, J.E.2    Foster, D.B.3
  • 34
    • 30944449043 scopus 로고    scopus 로고
    • Mitochondrial modulation: reversible phosphorylation takes center stage?
    • Pagliarini, D.J., and J.E. Dixon. 2006. Mitochondrial modulation: reversible phosphorylation takes center stage? Trends Biochem. Sci. 31:26-34. http://dx.doi.org/10.1016/j.tibs.2005.11.005
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 26-34
    • Pagliarini, D.J.1    Dixon, J.E.2
  • 35
    • 34347230164 scopus 로고    scopus 로고
    • Measuring calcium signaling using genetically targetable fluorescent indicators
    • Palmer, A.E., and R.Y. Tsien. 2006. Measuring calcium signaling using genetically targetable fluorescent indicators. Nat. Protoc. 1:1057-1065. http://dx.doi.org/10.1038/nprot.2006.172
    • (2006) Nat. Protoc. , vol.1 , pp. 1057-1065
    • Palmer, A.E.1    Tsien, R.Y.2
  • 36
    • 0032511112 scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto, R., P. Pinton, W. Carrington, F.S. Fay, K.E. Fogarty, L.M. Lifshitz, R.A. Tuft, and T. Pozzan. 0998. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science. 280: 1763-1766. http://dx.doi.org/10.1126/science.280.5370.1763
    • (998) Science. , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3    Fay, F.S.4    Fogarty, K.E.5    Lifshitz, L.M.6    Tuft, R.A.7    Pozzan, T.8
  • 37
    • 0038482043 scopus 로고    scopus 로고
    • Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70
    • Robin, M.-A., S.K. Prabu, H. Raza, H.K. Anandatheerthavarada, and N.G. Avadhani. 2003. Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70. J. Biol. Chem. 278:18960-18970. http://dx.doi.org/10.1074/jbc.M301807200
    • (2003) J. Biol. Chem. , vol.278 , pp. 18960-18970
    • Robin, M.-A.1    Prabu, S.K.2    Raza, H.3    Anandatheerthavarada, H.K.4    Avadhani, N.G.5
  • 38
    • 33749469540 scopus 로고    scopus 로고
    • Occurrence of A-kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria
    • Sardanelli, A.M., A. Signorile, R. Nuzzi, D.D. Rasmo, Z. Technikova-Dobrova, Z. Drahota, A. Occhiello, A. Pica, and S. Papa. 2006. Occurrence of A-kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria. FEBS Lett. 580:5690-5696. http://dx.doi.org/10.1016/j.febslet.2006.09.020
    • (2006) FEBS Lett. , vol.580 , pp. 5690-5696
    • Sardanelli, A.M.1    Signorile, A.2    Nuzzi, R.3    Rasmo, D.D.4    Technikova-Dobrova, Z.5    Drahota, Z.6    Occhiello, A.7    Pica, A.8    Papa, S.9
  • 40
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax, J.A., and J.E. Ferrell Jr. 2007. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8:530-541. http://dx.doi.org/10.1038/nrm2203
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell, J.E.Jr.2
  • 41
    • 44849141908 scopus 로고    scopus 로고
    • A comparison of donor-acceptor pairs for genetically encoded FRET sensors: application to the Epac cAMP sensor as an example
    • van der Krogt, G.N.M., J. Ogink, B. Ponsioen, and K. Jalink. 2008. A comparison of donor-acceptor pairs for genetically encoded FRET sensors: application to the Epac cAMP sensor as an example. PLoS ONE. 3:e1916. http://dx.doi.org/10.1371/journal.pone.0001916
    • (2008) PLoS ONE. , vol.3
    • van der Krogt, G.N.M.1    Ogink, J.2    Ponsioen, B.3    Jalink, K.4
  • 42
    • 0035411545 scopus 로고    scopus 로고
    • Bicarbonate-regulated soluble adenylyl cyclase
    • Wuttke, M.S., J. Buck, and L.R. Levin. 2001. Bicarbonate-regulated soluble adenylyl cyclase. JOP. 2(4, Suppl):154-158.
    • (2001) JOP. , vol.2 , Issue.4 SUPPL , pp. 154-158
    • Wuttke, M.S.1    Buck, J.2    Levin, L.R.3
  • 43
    • 82255192443 scopus 로고    scopus 로고
    • Spatial control of cAMP signalling in health and disease
    • Zaccolo, M. 2011. Spatial control of cAMP signalling in health and disease. Curr. Opin. Pharmacol. 11:649-655. http://dx.doi.org/10.1016/j.coph.2011.09.014
    • (2011) Curr. Opin. Pharmacol. , vol.11 , pp. 649-655
    • Zaccolo, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.