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Volumn 491, Issue 7424, 2012, Pages 468-472

A bimodular mechanism of calcium control in eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALMODULIN; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84869097530     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11539     Document Type: Article
Times cited : (107)

References (28)
  • 1
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham, D. E. Calcium signaling. Cell 131, 1047-1058 (2007).
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 2
    • 0037022309 scopus 로고    scopus 로고
    • Calcium signaling: A tale for all seasons
    • Carafoli, E. Calcium signaling: a tale for all seasons. Proc. Natl Acad. Sci. USA 99, 1115-1122 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1115-1122
    • Carafoli, E.1
  • 3
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • Ghosh, A. & Greenberg, M. E. Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science 268, 239-247 (1995).
    • (1995) Science , vol.268 , pp. 239-247
    • Ghosh, A.1    Greenberg, M.E.2
  • 4
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calciumsignalling
    • Berridge, M. J. Inositol trisphosphate and calciumsignalling. Nature 361, 315-325 (1993).
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 5
    • 36749035512 scopus 로고    scopus 로고
    • Plasma-membrane Ca(21) pumps: Structural diversity as the basis for functional versatility
    • Strehler, E. E., Filoteo, A. G., Penniston, J. T. & Caride, A. J. Plasma-membrane Ca(21) pumps: structural diversity as the basis for functional versatility. Biochem. Soc. Trans. 35, 919-922 (2007).
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 919-922
    • Strehler, E.E.1    Filoteo, A.G.2    Penniston, J.T.3    Caride, A.J.4
  • 6
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini, M. & Carafoli, E. Calcium pumps in health and disease. Physiol. Rev. 89, 1341-1378 (2009).
    • (2009) Physiol. Rev. , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 7
    • 84863869646 scopus 로고    scopus 로고
    • The plasma membrane Ca21 ATPase and the plasma membrane sodiumcalciumexchanger cooperate in the regulation of cell calcium
    • Brini, M. & Carafoli, E. The plasma membrane Ca21 ATPase and the plasma membrane sodiumcalciumexchanger cooperate in the regulation of cell calcium. Cold Spring Harb. Perspect. Biol. 3, 1-15 (2011).
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 1-15
    • Brini, M.1    Carafoli, E.2
  • 8
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen, K. B. & Palmgren, M. G. Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101 (1998).
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 9
    • 0030614802 scopus 로고    scopus 로고
    • A calmodulin-stimulated Ca21- ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus
    • Malmström, S., Askerlund, P. & Palmgren, M. G. A calmodulin-stimulated Ca21- ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus. FEBS Lett. 400, 324-328 (1997).
    • (1997) FEBS Lett. , vol.400 , pp. 324-328
    • Malmström, S.1    Askerlund, P.2    Palmgren, M.G.3
  • 10
    • 0025922159 scopus 로고
    • The plasma membrane Ca21 pump contains a site that interacts with its calmodulin-binding domain
    • Falchetto, R., Vorherr, T., Brunner, J. & Carafoli, E. The plasma membrane Ca21 pump contains a site that interacts with its calmodulin-binding domain. J. Biol. Chem. 266, 2930-2936 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2930-2936
    • Falchetto, R.1    Vorherr, T.2    Brunner, J.3    Carafoli, E.4
  • 11
    • 0027069575 scopus 로고
    • The calmodulin-binding site of the plasma membrane Ca21 pump interacts with the transduction domain of the enzyme
    • Falchetto, R., Vorherr, T. & Carafoli, E. The calmodulin-binding site of the plasma membrane Ca21 pump interacts with the transduction domain of the enzyme. Protein Sci. 1, 1613-1621 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 12
    • 78649655549 scopus 로고    scopus 로고
    • Plant and animal type 2B Ca21-ATPases: Evidence for a common auto-inhibitory mechanism
    • Bonza, M. C. & Luoni, L. Plant and animal type 2B Ca21-ATPases: evidence for a common auto-inhibitory mechanism. FEBS Lett. 584, 4783-4788 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 4783-4788
    • Bonza, M.C.1    Luoni, L.2
  • 13
    • 0028113894 scopus 로고
    • Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli, E. Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8, 993-1002 (1994).
    • (1994) FASEB J. , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 14
    • 0032530540 scopus 로고    scopus 로고
    • Modulation of the plasma membrane Ca21 pump
    • Penniston, J. T. & Enyedi, A. Modulation of the plasma membrane Ca21 pump. J. Membr. Biol. 165, 101-109 (1998).
    • (1998) J. Membr. Biol. , vol.165 , pp. 101-109
    • Penniston, J.T.1    Enyedi, A.2
  • 15
    • 33644864126 scopus 로고    scopus 로고
    • The plant plasma membraneCa21pumpACA8contains overlapping aswell asphysically separated autoinhibitory and calmodulin-binding domains
    • Baekgaard, L., Luoni, L., De Michelis, M. I. & Palmgren, M. G. The plant plasma membraneCa21pumpACA8contains overlapping aswell asphysically separated autoinhibitory and calmodulin-binding domains. J. Biol. Chem. 281, 1058-1065 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 1058-1065
    • Baekgaard, L.1    Luoni, L.2    De Michelis, M.I.3    Palmgren, M.G.4
  • 16
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K. P. & Ikura, M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108, 739-742 (2002).
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 17
    • 77950473953 scopus 로고    scopus 로고
    • Calmodulin wraps around its binding domain in the plasma membrane Ca21 pump anchored by a novel 18-1 motif
    • Juranic, N. et al. Calmodulin wraps around its binding domain in the plasma membrane Ca21 pump anchored by a novel 18-1 motif. J. Biol. Chem. 285, 4015-4024 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 4015-4024
    • Juranic, N.1
  • 18
    • 78649648346 scopus 로고    scopus 로고
    • The solution structure of a plant calmodulin and the CaMbinding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism
    • Ishida, H. & Vogel, H. J. The solution structure of a plant calmodulin and the CaMbinding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism. J. Biol. Chem. 285, 38502-38510 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 38502-38510
    • Ishida, H.1    Vogel, H.J.2
  • 19
    • 0028079476 scopus 로고
    • Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca21 ATPases
    • Cunningham, K. W. & Fink, G. R. Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca21 ATPases. J. Cell Biol. 124, 351-363 (1994).
    • (1994) J. Cell Biol. , vol.124 , pp. 351-363
    • Cunningham, K.W.1    Fink, G.R.2
  • 20
    • 0031664331 scopus 로고    scopus 로고
    • The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca21 and Mn21 required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation
    • Durr, G. et al. The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca21 and Mn21 required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation. Mol. Biol. Cell 9, 1149-1162 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1149-1162
    • Durr, G.1
  • 21
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler, E. E. & Zacharias, D. A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81, 21-50 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 22
    • 0028177570 scopus 로고
    • TheCa21affinity of the plasmamembraneCa21pumpis controlled by alternative splicing
    • Enyedi, A. et al.TheCa21affinity of the plasmamembraneCa21pumpis controlled by alternative splicing. J. Biol. Chem. 269, 41-43 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 41-43
    • Enyedi, A.1
  • 23
    • 0027258001 scopus 로고
    • Alternative splicing of C-terminal tail of prostaglandin e receptor subtype EP3 determines G-protein specificity
    • Namba, T. et al. Alternative splicing of C-terminal tail of prostaglandin E receptor subtype EP3 determines G-protein specificity. Nature 365, 166-170 (1993).
    • (1993) Nature , vol.365 , pp. 166-170
    • Namba, T.1
  • 24
    • 0027240588 scopus 로고
    • Differential signal transduction by five splice variants of the PACAP receptor
    • Spengler, D. et al. Differential signal transduction by five splice variants of the PACAP receptor. Nature 365, 170-175 (1993).
    • (1993) Nature , vol.365 , pp. 170-175
    • Spengler, D.1
  • 25
    • 71449105949 scopus 로고    scopus 로고
    • Single point mutations in the small cytoplasmic loop of ACA8, a plasma membrane Ca21-ATPase of Arabidopsis thaliana, generate partially deregulated pumps
    • Fusca, T. et al. Single point mutations in the small cytoplasmic loop of ACA8, a plasma membrane Ca21-ATPase of Arabidopsis thaliana, generate partially deregulated pumps. J. Biol. Chem. 284, 30881-30888 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 30881-30888
    • Fusca, T.1
  • 26
    • 56849123631 scopus 로고    scopus 로고
    • Dual mechanismof activation of plant plasma membrane Ca21-ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps with the calmodulin-binding site
    • Meneghelli, S., Fusca, T., Luoni, L. & De Michelis, M. I.Dual mechanismof activation of plant plasma membrane Ca21-ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps with the calmodulin-binding site. Mol. Membr. Biol. 25, 539-546 (2008).
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 539-546
    • Meneghelli, S.1    Fusca, T.2    Luoni, L.3    De Michelis, M.I.4
  • 27
    • 77749285818 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of calmodulin in complex with the regulatory domain of the plasma-membrane Ca21-ATPase ACA8
    • Tidow, H., Hein, K. L., Baekgaard, L., Palmgren, M. G. & Nissen, P. Expression, purification, crystallization and preliminary X-ray analysis of calmodulin in complex with the regulatory domain of the plasma-membrane Ca21-ATPase ACA8. Acta Crystallogr. F 66, 361-363 (2010).
    • (2010) Acta Crystallogr. F , vol.66 , pp. 361-363
    • Tidow, H.1    Hein, K.L.2    Baekgaard, L.3    Palmgren, M.G.4    Nissen, P.5
  • 28
    • 3042601242 scopus 로고    scopus 로고
    • A plant plasma membrane Ca21 pump is required for normal pollen tube growth and fertilization
    • Schiott, M. et al. A plant plasma membrane Ca21 pump is required for normal pollen tube growth and fertilization. Proc. Natl Acad. Sci. USA 101, 9502-9507 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9502-9507
    • Schiott, M.1


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