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Volumn 14, Issue 2, 2013, Pages 97-110

Ca2+-sensor proteins in the autophagic and endocytic traffic

Author keywords

Autophagy; Calcium; Endocytosis; Lysosomes; Membrane fusion

Indexed keywords

1, 4 DIHYDRO 2, 6 DIMETHYL 5 NITRO 4 [2 (TRIFLUOROMETHYL) PHENYL] 3 PYRIDINECARBOXYLIC ACID METHYL ESTER; BECLIN 1; CALCINEURIN; CALCIUM ION; FLUSPIRILENE; MITOGEN ACTIVATED PROTEIN KINASE 3; NEURONAL CALCIUM SENSOR; PROTEIN BCL 2; THAPSIGARGIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; TRANSIENT RECEPTOR POTENTIAL CHANNEL 2; TRANSIENT RECEPTOR POTENTIAL CHANNEL 3; UNCLASSIFIED DRUG; VERAPAMIL;

EID: 84878620754     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/13892037112139990033     Document Type: Article
Times cited : (26)

References (143)
  • 2
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum
    • Mijaljica, D., M. Prescott, and R.J. Devenish, Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy, 2011, 7(7): 673-682.
    • (2011) Autophagy , vol.7 , Issue.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 3
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Selectivity pays off
    • Cuervo, A.M., Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol. Metab., 2010, 21(3), 142-150.
    • (2010) Trends Endocrinol. Metab , vol.21 , Issue.3 , pp. 142-150
    • Cuervo, A.M.1
  • 4
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B. and D.J. Klionsky. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell, 2004, 6(4): 463-477.
    • (2004) Dev. Cell , vol.6 , Issue.4 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 6
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • Mari, M.; Griffith, J.; Rieter, E.; Krishnappa, L.; Klionsky, D.J.; Reggiori, F. An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J. Cell Biol., 2010, 190(6): 1005-1022.
    • (2010) J. Cell Biol , vol.190 , Issue.6 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krishnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 7
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of preautophagosomal structures
    • Ravikumar, B.; Moreau, K; Jahreiss, L; Puri, C; Rubinsztein, D. C. Plasma membrane contributes to the formation of preautophagosomal structures. Nat. Cell Biol., 2010, 12(8): 747-757.
    • (2010) Nat. Cell Biol , vol.12 , Issue.8 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 9
    • 84869459702 scopus 로고    scopus 로고
    • Recycling endosomes contribute to autophagosome formation
    • Longatti, A. and S.A. Tooze. Recycling endosomes contribute to autophagosome formation. Autophagy, 2012, 8(11).
    • (2012) Autophagy , vol.8 , Issue.11
    • Longatti, A.1    Tooze, S.A.2
  • 10
    • 77955165003 scopus 로고    scopus 로고
    • The plasma membrane brings autophagosomes to life
    • Cuervo, A.M. The plasma membrane brings autophagosomes to life. Nat. Cell Biol., 2010, 12(8), 735-737.
    • (2010) Nat. Cell Biol , vol.12 , Issue.8 , pp. 735-737
    • Cuervo, A.M.1
  • 11
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E.L., Walker, S. A.; Manifava, M.; Chandra, P.; Roderick, H. L., Habermann, A.; Griffiths, G.; Ktistakis, N. T. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol., 2008, 182(4), 685-701.
    • (2008) J. Cell Biol , vol.182 , Issue.4 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 12
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • Hayashi-Nishino, M.; Fujita, N.; Noda, T.; Yamaguchi, A.; Yoshimori, T.; Yamamoto, A. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat. Cell Biol., 2009, 11(12), 1433-1437.
    • (2009) Nat. Cell Biol , vol.11 , Issue.12 , pp. 1433-1437
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3    Yamaguchi, A.4    Yoshimori, T.5    Yamamoto, A.6
  • 13
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Anttila, P.; Vihinen, H.; Jokitalo, E.; Eskelinen, E. L. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy, 2009, 5(8), 1180-1185.
    • (2009) Autophagy , vol.5 , Issue.8 , pp. 1180-1185
    • Yla-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.L.4
  • 14
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: How does the end begin?
    • Noda, T., N. Fujita, and T. Yoshimori. The late stages of autophagy: how does the end begin? Cell Death Differ., 2009, 16(7), 984-990.
    • (2009) Cell Death Differ , vol.16 , Issue.7 , pp. 984-990
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 16
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • Mizushima, N., T. Yoshimori, and Y. Ohsumi, The role of Atg proteins in autophagosome formation. Annu. Rev. Cell Dev. Biol., 2011, 27(10): 107-132.
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , Issue.10 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 18
    • 47749107873 scopus 로고    scopus 로고
    • Shaping cups into phagosomes and macropinosomes
    • Swanson, J. A. Shaping cups into phagosomes and macropinosomes. Nat Rev Mol. Cell Biol., 2008, 9(8), 639-649.
    • (2008) Nat Rev Mol. Cell Biol , vol.9 , Issue.8 , pp. 639-649
    • Swanson, J.A.1
  • 19
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: Two closely related partners
    • Fader, C.M. and M.I. Colombo, Autophagy and multivesicular bodies: two closely related partners. Cell Death Differ., 2009, 16(1), 70-78.
    • (2009) Cell Death Differ , vol.16 , Issue.1 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 20
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling: Dynamics, homeostasis and remodelling
    • Berridge, M. J.; M.D. Bootman, and H.L. Roderick. Calcium signalling: dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol., 2003, 4(7): 517-529.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , Issue.7 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 24
    • 77950575506 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism
    • Vingtdeux, V., et al., AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism. J. Biol. Chem., 2010, 285(12): 9100-9113.
    • (2010) J. Biol. Chem , vol.285 , Issue.12 , pp. 9100-9113
    • Vingtdeux, V.1
  • 25
    • 47249094223 scopus 로고    scopus 로고
    • Role of non-canonical Beclin 1-independent autophagy in cell death induced by resveratrol in human breast cancer cells
    • Scarlatti, F.; Maffei, R; Beau, I.; Codogno, P.; Ghidoni, R. Role of non-canonical Beclin 1-independent autophagy in cell death induced by resveratrol in human breast cancer cells. Cell Death Differ., 2008, 15(8), 1318-1329.
    • (2008) Cell Death Differ , vol.15 , Issue.8 , pp. 1318-1329
    • Scarlatti, F.1    Maffei, R.2    Beau, I.3    Codogno, P.4    Ghidoni, R.5
  • 26
    • 81555210958 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent kinase (CaMK) signaling via CaMKI and AMP-activated protein kinase contributes to the regulation of WIPI-1 at the onset of autophagy
    • Pfisterer, S. G.; Mauthe, M.; Codogno, P.; Proikas-Cezanne, T. Ca2+/calmodulin-dependent kinase (CaMK) signaling via CaMKI and AMP-activated protein kinase contributes to the regulation of WIPI-1 at the onset of autophagy. Mol. Pharmacol., 2011, 80(6), 1066-1075.
    • (2011) Mol. Pharmacol , vol.80 , Issue.6 , pp. 1066-1075
    • Pfisterer, S.G.1    Mauthe, M.2    Codogno, P.3    Proikas-Cezanne, T.4
  • 27
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • Gao, W.; Ding, W. X.; Stolz, D. B.; Yin, X. M. Induction of macroautophagy by exogenously introduced calcium. Autophagy, 2008, 4(6), 754-761.
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3    Yin, X.M.4
  • 30
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • Gordon, P.B.; Holen, I.; Fosse, M.; Røtnes, J. S.; Seglen, P. O. Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J. Biol. Chem., 1993, 268(35), 26107-26112.
    • (1993) J. Biol. Chem , vol.268 , Issue.35 , pp. 26107-26112
    • Gordon, P.B.1    Holen, I.2    Fosse, M.3    Røtnes, J.S.4    Seglen, P.O.5
  • 31
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signaling organelle
    • Berridge, M. J. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium, 2002, 32(5-6), 235-249.
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 235-249
    • Berridge, M.J.1
  • 32
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales, S.; F.R. Papa, and P. Walter. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol., 2006, 22, 487-508.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 33
    • 33646267694 scopus 로고    scopus 로고
    • Conformational diseases and ER stress-mediated cell death: Apoptotic cell death and autophagic cell death
    • Momoi, T. Conformational diseases and ER stress-mediated cell death: apoptotic cell death and autophagic cell death. Curr. Mol. Med., 2006, 6(1): 111-118.
    • (2006) Curr. Mol. Med , vol.6 , Issue.1 , pp. 111-118
    • Momoi, T.1
  • 35
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup, O.; Cullen, P. J.; Drøbak, B. K.; Hanley, M. R.; Dawson, A. P. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc. Natl. Acad. Sci. USA., 1990, 87(7), 2466-2470.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.7 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drøbak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 36
    • 81555210958 scopus 로고    scopus 로고
    • Ca2+/Calmodulin-dependent Kinase Signaling via CaMKI and AMPK Contributes to the Regulation of WIPI-1 at the Onset of Autophagy
    • Pfisterer, S.G.; Mauthe, M.; Codogno, P.; Proikas-Cezanne, T. Ca2+/Calmodulin-dependent Kinase Signaling via CaMKI and AMPK Contributes to the Regulation of WIPI-1 at the Onset of Autophagy. Mol. Pharmacol., 2011.
    • (2011) Mol. Pharmacol
    • Pfisterer, S.G.1    Mauthe, M.2    Codogno, P.3    Proikas-Cezanne, T.4
  • 37
    • 66049132843 scopus 로고    scopus 로고
    • The ER and ageing II: Calcium homeostasis
    • Puzianowska-Kuznicka, M. and J. Kuznicki. The ER and ageing II: calcium homeostasis. Ageing Res. Rev., 2009, 8(3), 160-172.
    • (2009) Ageing Res. Rev , vol.8 , Issue.3 , pp. 160-172
    • Puzianowska-Kuznicka, M.1    Kuznicki, J.2
  • 38
    • 47249157360 scopus 로고    scopus 로고
    • Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum
    • Sakaki, K.; J. Wu, and R. J. Kaufman. Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum. J. Biol. Chem., 2008, 283(22), 15370-15380.
    • (2008) J. Biol. Chem , vol.283 , Issue.22 , pp. 15370-15380
    • Sakaki, K.1    Wu, J.2    Kaufman, R.J.3
  • 39
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Hoyer-Hansen, M. and M. Jaattela. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ., 2007, 14(9), 1576-1582.
    • (2007) Cell Death Differ , vol.14 , Issue.9 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 40
    • 39449105425 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptor is required to signal autophagic cell death
    • Lam, D.; Kosta, A.; Luciani, M. F.; Golstein, P. The inositol 1,4,5-trisphosphate receptor is required to signal autophagic cell death. Mol. Biol. Cell, 2008, 19(2), 691-700.
    • (2008) Mol. Biol. Cell , vol.19 , Issue.2 , pp. 691-700
    • Lam, D.1    Kosta, A.2    Luciani, M.F.3    Golstein, P.4
  • 42
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J.; Kundu, M.; Viollet, B.; Guan, K. L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol., 2011, 13(2), 132-141.
    • (2011) Nat. Cell Biol , vol.13 , Issue.2 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 43
    • 35348972413 scopus 로고    scopus 로고
    • Uridine-5'-triphosphate (UTP) maintains cardiac mitochondrial function following chemical and hypoxic stress
    • Yitzhaki, S.; Hochhauser, E.; Porat, E.; Shainberg, A. Uridine-5'-triphosphate (UTP) maintains cardiac mitochondrial function following chemical and hypoxic stress. J. Mol. Cell Cardiol., 43(5), 653-662.
    • J. Mol. Cell Cardiol , vol.43 , Issue.5 , pp. 653-662
    • Yitzhaki, S.1    Hochhauser, E.2    Porat, E.3    Shainberg, A.4
  • 44
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • Ganley, I.G.; Wong, P. M.; Gammoh, N.; Jiang, X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol. Cell, 2011, 42(6), 731-743.
    • (2011) Mol. Cell , vol.42 , Issue.6 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 45
    • 81555210958 scopus 로고    scopus 로고
    • Ca2+/Calmodulin-dependent Kinase Signaling via CaMKI and AMPK Contributes to the Regulation of WIPI-1 at the Onset of Autophagy
    • Pfisterer, S.G.; Mauthe, M.; Codogno, P.; Proikas-Cezanne, T. Ca2+/Calmodulin-dependent Kinase Signaling via CaMKI and AMPK Contributes to the Regulation of WIPI-1 at the Onset of Autophagy. Mol. Pharmacol., 2011, 80(6), 1066-1075.
    • (2011) Mol. Pharmacol , vol.80 , Issue.6 , pp. 1066-1075
    • Pfisterer, S.G.1    Mauthe, M.2    Codogno, P.3    Proikas-Cezanne, T.4
  • 46
    • 33645633094 scopus 로고    scopus 로고
    • Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses
    • Dode, L.; Andersen, J. P.; Vanoevelen, J.; Raeymaekers, L.; Missiaen, L.; Vilsen, B.; Wuytack, F. Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses. J. Biol. Chem., 2006, 281(6), 3182-3189.
    • (2006) J. Biol. Chem , vol.281 , Issue.6 , pp. 3182-3189
    • Dode, L.1    Andersen, J.P.2    Vanoevelen, J.3    Raeymaekers, L.4    Missiaen, L.5    Vilsen, B.6    Wuytack, F.7
  • 47
    • 3943105516 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptors as signal integrators
    • Patterson, R.L.; D. Boehning, and S.H. Snyder. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annu. Rev. Biochem., 2004, 73, 437-465.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 437-465
    • Patterson, R.L.1    Boehning, D.2    Snyder, S.H.3
  • 52
    • 77952759763 scopus 로고    scopus 로고
    • Role of inositol trisphosphate receptors in autophagy in DT40 cells
    • Khan, M.T. and S.K. Joseph, Role of inositol trisphosphate receptors in autophagy in DT40 cells. J. Biol. Chem., 2010, 285(22), 16912-16920.
    • (2010) J. Biol. Chem , vol.285 , Issue.22 , pp. 16912-16920
    • Khan, M.T.1    Joseph, S.K.2
  • 53
    • 77957662227 scopus 로고    scopus 로고
    • Glucocorticoids downregulate Fyn and inhibit IP(3)-mediated calcium signaling to promote autophagy in T lymphocytes
    • Harr, M.W.; McColl, K. S.; Zhong, F.; Molitoris, J. K.; Distelhorst, C. W. Glucocorticoids downregulate Fyn and inhibit IP(3)-mediated calcium signaling to promote autophagy in T lymphocytes. Autophagy, 2010, 6(7), 912-921.
    • (2010) Autophagy , vol.6 , Issue.7 , pp. 912-921
    • Harr, M.W.1    McColl, K.S.2    Zhong, F.3    Molitoris, J.K.4    Distelhorst, C.W.5
  • 56
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • Zalckvar, E.; Berissi, H.; Mizrachy, L.; Idelchuk, Y.; Koren, I.; Eisenstein, M.; Sabanay, H.; Pinkas-Kramarski, R.; Kimchi, A. DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep., 2009, 10(3), 285-292.
    • (2009) EMBO Rep , vol.10 , Issue.3 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3    Idelchuk, Y.4    Koren, I.5    Eisenstein, M.6    Sabanay, H.7    Pinkas-Kramarski, R.8    Kimchi, A.9
  • 57
    • 67650270918 scopus 로고    scopus 로고
    • Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL
    • Zalckvar, E.; Berissi, H.; Eisenstein, M.; Kimchi, A. Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL. Autophagy, 2009, 5(5), 720-722.
    • (2009) Autophagy , vol.5 , Issue.5 , pp. 720-722
    • Zalckvar, E.1    Berissi, H.2    Eisenstein, M.3    Kimchi, A.4
  • 58
    • 76349114046 scopus 로고    scopus 로고
    • Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1
    • Chang, N.C.; Nguyen, M.; Germain, M.; Shore, G. C. Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1. Embo J., 2010, 29(3), 606-618.
    • (2010) Embo J , vol.29 , Issue.3 , pp. 606-618
    • Chang, N.C.1    Nguyen, M.2    Germain, M.3    Shore, G.C.4
  • 59
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the BclXL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • Oberstein, A.; P.D. Jeffrey, and Y. Shi. Crystal structure of the BclXL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J. Biol. Chem., 2007, 282(17), 13123-13132.
    • (2007) J. Biol. Chem , vol.282 , Issue.17 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 60
    • 34547689505 scopus 로고    scopus 로고
    • Molecular basis of BclxL's target recognition versatility revealed by the structure of BclxL in complex with the BH3 domain of Beclin-1
    • Feng, W.; Huang, S.; Wu, H.; Zhang, M. Molecular basis of BclxL's target recognition versatility revealed by the structure of BclxL in complex with the BH3 domain of Beclin-1. J. Mol. Biol., 2007, 372(1), 223-235.
    • (2007) J. Mol. Biol , vol.372 , Issue.1 , pp. 223-235
    • Feng, W.1    Huang, S.2    Wu, H.3    Zhang, M.4
  • 62
    • 47349099011 scopus 로고    scopus 로고
    • Bcl-2 suppresses Ca2+ release through inositol 1.;4.;5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content
    • Hanson, C. J.; Bootman, M. D.; Distelhorst, C. W.; Wojcikiewicz, R. J.; Roderick, H. L. Bcl-2 suppresses Ca2+ release through inositol 1.;4.;5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content. Cell Calcium., 2008, 44(3), 324-338.
    • (2008) Cell Calcium , vol.44 , Issue.3 , pp. 324-338
    • Hanson, C.J.1    Bootman, M.D.2    Distelhorst, C.W.3    Wojcikiewicz, R.J.4    Roderick, H.L.5
  • 63
    • 10644234677 scopus 로고    scopus 로고
    • Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor
    • Palmer, A.E.; Jin, C.; Reed, J. C.; Tsien, R. Y. Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor. Proc. Natl. Acad. Sci. USA., 2004, 101(50), 17404-17409.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.50 , pp. 17404-17409
    • Palmer, A.E.1    Jin, C.2    Reed, J.C.3    Tsien, R.Y.4
  • 65
    • 56549125810 scopus 로고    scopus 로고
    • Cadmium-induced autophagy and apoptosis are mediated by a calcium signaling pathway
    • Wang, S. H.; Shih, Y. L.; Ko, W. C.; Wei, Y. H.; Shih, C. M. Cadmium-induced autophagy and apoptosis are mediated by a calcium signaling pathway. Cell Mol. Life Sci.; 2008, 65(22), 3640-3652.
    • (2008) Cell Mol. Life Sci , vol.65 , Issue.22 , pp. 3640-3652
    • Wang, S.H.1    Shih, Y.L.2    Ko, W.C.3    Wei, Y.H.4    Shih, C.M.5
  • 66
    • 0035133762 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate affects the inositol 1.;4.;5-trisphosphate receptor.; the intracellular Ca2+ pump and the nonspecific Ca2+ leak from the non-mitochondrial Ca2+ stores in permeabilized A7r5 cells
    • Missiaen, L.; Callewaert, G.; De Smedt, H.; Parys, J. B. 2-Aminoethoxydiphenyl borate affects the inositol 1.;4.;5-trisphosphate receptor.; the intracellular Ca2+ pump and the nonspecific Ca2+ leak from the non-mitochondrial Ca2+ stores in permeabilized A7r5 cells. Cell Calcium, 2001, 29(2), 111-116.
    • (2001) Cell Calcium , vol.29 , Issue.2 , pp. 111-116
    • Missiaen, L.1    Callewaert, G.2    de Smedt, H.3    Parys, J.B.4
  • 67
    • 0035984392 scopus 로고    scopus 로고
    • Inhibition of SERCA Ca2+ pumps by 2-aminoethoxydiphenyl borate (2-APB). 2-APB reduces both Ca2+ binding and phosphoryl transfer from ATP.; by interfering with the pathway leading to the Ca2+-binding sites
    • Bilmen, J. G.; Wootton, L. L.; Godfrey, R. E.; Smart, O. S.; Michelangeli, F. Inhibition of SERCA Ca2+ pumps by 2-aminoethoxydiphenyl borate (2-APB). 2-APB reduces both Ca2+ binding and phosphoryl transfer from ATP.; by interfering with the pathway leading to the Ca2+-binding sites. Eur. J. Biochem., 2002, 269(15), 3678-3687.
    • (2002) Eur. J. Biochem , vol.269 , Issue.15 , pp. 3678-3687
    • Bilmen, J.G.1    Wootton, L.L.2    Godfrey, R.E.3    Smart, O.S.4    Michelangeli, F.5
  • 68
    • 0037404976 scopus 로고    scopus 로고
    • Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs
    • Sugden, M. C. and M. J. Holness. Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs. Am J Physiol Endocrinol Metab., 2003, 284(5), E855-E862.
    • (2003) Am J Physiol Endocrinol Metab , vol.284 , Issue.5
    • Sugden, M.C.1    Holness, M.J.2
  • 69
    • 68649092333 scopus 로고    scopus 로고
    • The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work
    • Balaban, R. S. The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work. Biochim Biophys Acta.; 2009. 1787(11), 1334-41.
    • (2009) Biochim Biophys Acta , vol.1787 , Issue.11 , pp. 1334-1341
    • Balaban, R.S.1
  • 70
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: The hub of cellular Ca2+ signaling
    • Szabadkai, G. and M. R. Duchen. Mitochondria: the hub of cellular Ca2+ signaling. Physiology (Bethesda)., 2008, 23(2), 84-94.
    • (2008) Physiology (Bethesda) , vol.23 , Issue.2 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 71
    • 4043086952 scopus 로고    scopus 로고
    • Mitochondria in health and disease: Perspectives on a new mitochondrial biology
    • Duchen, M. R. Mitochondria in health and disease: perspectives on a new mitochondrial biology. Mol. Aspects Med., 2004, 25(4), 365-451.
    • (2004) Mol. Aspects Med , vol.25 , Issue.4 , pp. 365-451
    • Duchen, M.R.1
  • 72
    • 44749089373 scopus 로고    scopus 로고
    • High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling
    • Spat, A.; Szanda, G.; Csordás, G.; Hajnóczky, G. High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling. Cell Calcium, 2008, 44(1), 51-63.
    • (2008) Cell Calcium , vol.44 , Issue.1 , pp. 51-63
    • Spat, A.1    Szanda, G.2    Csordás, G.3    Hajnóczky, G.4
  • 74
    • 34247549679 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis
    • Rasola, A. and P. Bernardi. The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis. Apoptosis, 2007, 12(5), 815-833.
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 815-833
    • Rasola, A.1    Bernardi, P.2
  • 75
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • Elmore, S. P.; Qian, T.; Grissom, S. F.; Lemasters, J. J. The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J.; 2001, 15(12), 2286-2287.
    • (2001) FASEB J , vol.15 , Issue.12 , pp. 2286-2287
    • Elmore, S.P.1    Qian, T.2    Grissom, S.F.3    Lemasters, J.J.4
  • 77
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death.; autophagy.; and mitophagy
    • Zhang, J. and P.A. Ney. Role of BNIP3 and NIX in cell death.; autophagy.; and mitophagy. Cell Death Differ., 2009, 16(7), 939-946.
    • (2009) Cell Death Differ , vol.16 , Issue.7 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 81
    • 0030589362 scopus 로고    scopus 로고
    • Activation of nuclear factor-kappaB via T cell receptor requires a Raf kinase and Ca2+ influx. Functional synergy between Raf and calcineurin
    • Kanno, T.; and U. Siebenlist. Activation of nuclear factor-kappaB via T cell receptor requires a Raf kinase and Ca2+ influx. Functional synergy between Raf and calcineurin. J. Immunol.; 1996, 157(12), 5277-5283.
    • (1996) J. Immunol , vol.157 , Issue.12 , pp. 5277-5283
    • Kanno, T.1    Siebenlist, U.2
  • 83
    • 36749070036 scopus 로고    scopus 로고
    • The role of calcium and other ions in sorting and delivery in the late endocytic pathway
    • Luzio, J. P.; N. A. Bright and P. R. Pryor. The role of calcium and other ions in sorting and delivery in the late endocytic pathway. Biochem. Soc. Trans., 2007, 35(Pt 5), 1088-1091.
    • (2007) Biochem. Soc. Trans , vol.35 , Issue.Pt 5 , pp. 1088-1091
    • Luzio, J.P.1    Bright, N.A.2    Pryor, P.R.3
  • 84
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor, P. R.; Mullock, B. M.; Bright, N. A.; Gray, S. R.; Luzio, J. P. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol., 2000, 149(5), 1053-1062.
    • (2000) J. Cell Biol , vol.149 , Issue.5 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 85
    • 52549098624 scopus 로고    scopus 로고
    • Membrane fusion: SNAREs and regulation
    • Malsam, J.; Kreye, S.; and T.H. Sollner. Membrane fusion: SNAREs and regulation. Cell Mol. Life Sci., 2008, 65(18), 2814-2832.
    • (2008) Cell Mol. Life Sci , vol.65 , Issue.18 , pp. 2814-2832
    • Malsam, J.1    Kreye, S.2    Sollner, T.H.3
  • 86
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens.; S. and H.T. McMahon. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol., 2008, 9(7), 543-556.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , Issue.7 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 87
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs--engines for membrane fusion
    • Jahn, R. and R.H. Scheller. SNAREs--engines for membrane fusion. Nat. Rev. Mol. Cell Biol., 2006, 7(9), 631-643.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , Issue.9 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 89
    • 2342661960 scopus 로고    scopus 로고
    • Phosphoinositides in constitutive membrane traffic
    • Roth, M. G. Phosphoinositides in constitutive membrane traffic. Physiol. Rev., 2004, 84(3), 699-730.
    • (2004) Physiol. Rev , vol.84 , Issue.3 , pp. 699-730
    • Roth, M.G.1
  • 90
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: A fundamental regulator of intracellular membrane fusion?
    • Hay, J. C. Calcium: a fundamental regulator of intracellular membrane fusion? EMBO Rep., 2007, 8(3), 236-240.
    • (2007) EMBO Rep , vol.8 , Issue.3 , pp. 236-240
    • Hay, J.C.1
  • 92
    • 0034988109 scopus 로고    scopus 로고
    • Relationships between EEA1 binding partners and their role in endosome fusion
    • Mills, I. G.; Urbe, S.; and M. J. Clague. Relationships between EEA1 binding partners and their role in endosome fusion. J. Cell Sci., 2001, 114(Pt 10), 1959-1965.
    • (2001) J. Cell Sci , vol.114 , Issue.Pt 10 , pp. 1959-1965
    • Mills, I.G.1    Urbe, S.2    Clague, M.J.3
  • 93
    • 0032506349 scopus 로고    scopus 로고
    • Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • Peters, C. and A. Mayer. Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature, 1998, 396(6711), 575-580.
    • (1998) Nature , vol.396 , Issue.6711 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 94
    • 0025947123 scopus 로고
    • Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse
    • Adler, E. M.; Augustine, G. J.; Duffy, S. N.; Charlton, M. P. Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse. J. Neurosci., 1991, 11(6), 1496-1507.
    • (1991) J. Neurosci , vol.11 , Issue.6 , pp. 1496-1507
    • Adler, E.M.1    Augustine, G.J.2    Duffy, S.N.3    Charlton, M.P.4
  • 95
    • 0042160096 scopus 로고    scopus 로고
    • Calcium and calmodulin in membrane fusion
    • Burgoyne, R. D. and M. J. Clague. Calcium and calmodulin in membrane fusion. Biochim. Biophys. Acta., 2003, 1641(2-3), 137-143.
    • (2003) Biochim. Biophys. Acta , vol.1641 , Issue.2-3 , pp. 137-143
    • Burgoyne, R.D.1    Clague, M.J.2
  • 96
    • 0032824099 scopus 로고    scopus 로고
    • Fusion of endosomes involved in synaptic vesicle recycling
    • Holroyd, C.; Kistner, U.; Annaert, W.; Jahn, R. Fusion of endosomes involved in synaptic vesicle recycling. Mol. Biol. Cell, 1999, 10(9), 3035-3044.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.9 , pp. 3035-3044
    • Holroyd, C.1    Kistner, U.2    Annaert, W.3    Jahn, R.4
  • 97
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M. I.; W. Beron, and P. D. Stahl. Calmodulin regulates endosome fusion. J. Biol. Chem., 1997, 272(12), 7707-7712.
    • (1997) J. Biol. Chem , vol.272 , Issue.12 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 98
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride.; H.M.; Rybin V.; Murphy C.; Giner A.; Teasdale R.; Zerial M. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell, 1999, 98(3), 377-386.
    • (1999) Cell , vol.98 , Issue.3 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 99
    • 73649127260 scopus 로고    scopus 로고
    • Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1
    • Vergarajauregui, S.; J. A. Martina, and R. Puertollano. Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1. J. Biol. Chem., 2009, 284(52), 36357-36366.
    • (2009) J. Biol. Chem , vol.284 , Issue.52 , pp. 36357-36366
    • Vergarajauregui, S.1    Martina, J.A.2    Puertollano, R.3
  • 101
    • 18744363612 scopus 로고    scopus 로고
    • Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV.; a disorder affecting the lysosomal pathway
    • LaPlante, J. M.; Falardeau, J.; Sun, M.; Kanazirska, M.; Brown, E. M.; Slaugenhaupt, S. A.; Vassilev, P. M. Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV.; a disorder affecting the lysosomal pathway. FEBS Lett., 2002, 532(1-2), 183-187.
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 183-187
    • Laplante, J.M.1    Falardeau, J.2    Sun, M.3    Kanazirska, M.4    Brown, E.M.5    Slaugenhaupt, S.A.6    Vassilev, P.M.7
  • 102
    • 36749008553 scopus 로고    scopus 로고
    • Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice
    • Xu, H.; Delling, M.; Li, L.; Dong, X.; Clapham, D. E. Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice. Proc. Natl. Acad. Sci. USA., 2007, 104(46), 18321-18326.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.46 , pp. 18321-18326
    • Xu, H.1    Delling, M.2    Li, L.3    Dong, X.4    Clapham, D.E.5
  • 103
    • 1842428593 scopus 로고    scopus 로고
    • Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis
    • Treusch, S.; Knuth, S.; Slaugenhaupt, S. A.; Goldin, E.; Grant, B. D.; Fares, H. Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis. Proc. Natl. Acad. Sci. USA., 2004, 101(13), 4483-4488.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.13 , pp. 4483-4488
    • Treusch, S.1    Knuth, S.2    Slaugenhaupt, S.A.3    Goldin, E.4    Grant, B.D.5    Fares, H.6
  • 105
    • 77956911289 scopus 로고    scopus 로고
    • Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy
    • Zeevi, D. A.; Lev, S.; Frumkin, A.; Minke, B.; Bach, G. Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy. J. Cell Sci., 2010, 123(Pt 18), 3112-3124.
    • (2010) J. Cell Sci , vol.123 , Issue.Pt 18 , pp. 3112-3124
    • Zeevi, D.A.1    Lev, S.2    Frumkin, A.3    Minke, B.4    Bach, G.5
  • 106
    • 84863317314 scopus 로고    scopus 로고
    • Role of TRPML and Two-Pore Channels in Endolysosomal Cation Homeostasis
    • Grimm, C.; Hassan, S.; Wahl-Schott, C.; Biel, M. Role of TRPML and Two-Pore Channels in Endolysosomal Cation Homeostasis. J. Pharmacol. Exp. Ther., 2012, 342(2), 236-244.
    • (2012) J. Pharmacol. Exp. Ther , vol.342 , Issue.2 , pp. 236-244
    • Grimm, C.1    Hassan, S.2    Wahl-Schott, C.3    Biel, M.4
  • 108
    • 0036253107 scopus 로고    scopus 로고
    • SKD1 AAA ATPase-dependent endosomal transport is involved in autolysosome formation
    • Nara, A.; Mizushima, N.; Yamamoto, A.; Kabeya, Y.; Ohsumi, Y.; Yoshimori, T. SKD1 AAA ATPase-dependent endosomal transport is involved in autolysosome formation. Cell Struct. Funct., 2002, 27(1), 29-37.
    • (2002) Cell Struct. Funct , vol.27 , Issue.1 , pp. 29-37
    • Nara, A.1    Mizushima, N.2    Yamamoto, A.3    Kabeya, Y.4    Ohsumi, Y.5    Yoshimori, T.6
  • 111
    • 45149103982 scopus 로고    scopus 로고
    • Membrane traffic and turnover in TRP-ML1-deficient cells: A revised model for mucolipidosis type IV pathogenesis
    • Miedel, M.T.; Rbaibi, Y.; Guerriero, C. J.; Colletti, G.; Weixel, K. M.; Weisz, O. A.; Kiselyov, K. Membrane traffic and turnover in TRP-ML1-deficient cells: a revised model for mucolipidosis type IV pathogenesis. J. Exp. Med.; 2008, 205(6), 1477-1490.
    • (2008) J. Exp. Med , vol.205 , Issue.6 , pp. 1477-1490
    • Miedel, M.T.1    Rbaibi, Y.2    Guerriero, C.J.3    Colletti, G.4    Weixel, K.M.5    Weisz, O.A.6    Kiselyov, K.7
  • 115
    • 38349104748 scopus 로고    scopus 로고
    • The varitint-waddler (Va) deafness mutation in TRPML3 generates constitutive.; inward rectifying currents and causes cell degeneration
    • Nagata, K.; Zheng, L.; Madathany, T.; Castiglioni, A. J.; Bartles, J. R.; García-Añoveros, J. The varitint-waddler (Va) deafness mutation in TRPML3 generates constitutive.; inward rectifying currents and causes cell degeneration. Proc. Natl. Acad. Sci. USA., 2008, 105(1), 353-358.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.1 , pp. 353-358
    • Nagata, K.1    Zheng, L.2    Madathany, T.3    Castiglioni, A.J.4    Bartles, J.R.5    García-Añoveros, J.6
  • 116
    • 37649014647 scopus 로고    scopus 로고
    • A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse
    • Grimm, C.; Cuajungco, M. P.; van Aken, A. F.; Schnee, M.; Jörs, S.; Kros, C. J.; Ricci, A. J.; Heller, S. A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse. Proc. Natl. Acad. Sci. USA., 2007, 104(49), 19583-19588.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.49 , pp. 19583-19588
    • Grimm, C.1    Cuajungco, M.P.2    van Aken, A.F.3    Schnee, M.4    Jörs, S.5    Kros, C.J.6    Ricci, A.J.7    Heller, S.8
  • 117
    • 33745193718 scopus 로고    scopus 로고
    • Lysosomal localization of TRPML3 depends on TRPML2 and the mucolipidosis-associated protein TRPML1
    • Venkatachalam, K.; T. Hofmann; and C. Montell. Lysosomal localization of TRPML3 depends on TRPML2 and the mucolipidosis-associated protein TRPML1. J. Biol. Chem., 2006, 281(25), 17517-17527.
    • (2006) J. Biol. Chem , vol.281 , Issue.25 , pp. 17517-17527
    • Venkatachalam, K.1    Hofmann, T.2    Montell, C.3
  • 118
    • 67649870315 scopus 로고    scopus 로고
    • The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy
    • Kim, H. J.; Soyombo, A. A.; Tjon-Kon-Sang, S.; So, I.; Muallem, S. The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy. Traffic, 2009, 10(8), 1157-1167.
    • (2009) Traffic , vol.10 , Issue.8 , pp. 1157-1167
    • Kim, H.J.1    Soyombo, A.A.2    Tjon-Kon-Sang, S.3    So, I.4    Muallem, S.5
  • 119
    • 67649882769 scopus 로고    scopus 로고
    • The calcium channel mucolipin-3 is a novel regulator of trafficking along the endosomal pathway
    • Martina, J. A.; B. Lelouvier, and R. Puertollano. The calcium channel mucolipin-3 is a novel regulator of trafficking along the endosomal pathway. Traffic, 2009, 10(8), 1143-1156.
    • (2009) Traffic , vol.10 , Issue.8 , pp. 1143-1156
    • Martina, J.A.1    Lelouvier, B.2    Puertollano, R.3
  • 124
    • 33845602018 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes
    • Beck, A.; Kolisek, M.; Bagley, L. A.; Fleig, A.; Penner, R. Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes. FASEB J., 2006, 20(7), 962-964.
    • (2006) FASEB J , vol.20 , Issue.7 , pp. 962-964
    • Beck, A.1    Kolisek, M.2    Bagley, L.A.3    Fleig, A.4    Penner, R.5
  • 126
    • 0037184523 scopus 로고    scopus 로고
    • NAADP mobilizes Ca(2+) from reserve granules.; lysosome-related organelles.; in sea urchin eggs
    • Churchill, G. C.; Okada, Y.; Thomas, J. M.; Genazzani, A. A.; Patel, S.; Galione, A. NAADP mobilizes Ca(2+) from reserve granules.; lysosome-related organelles.; in sea urchin eggs. Cell, 2002, 111(5), 703-708.
    • (2002) Cell , vol.111 , Issue.5 , pp. 703-708
    • Churchill, G.C.1    Okada, Y.2    Thomas, J.M.3    Genazzani, A.A.4    Patel, S.5    Galione, A.6
  • 127
    • 77955789211 scopus 로고    scopus 로고
    • Altered lipid content inhibits autophagic vesicular fusion
    • Koga, H.; S. Kaushik.; and A.M. Cuervo. Altered lipid content inhibits autophagic vesicular fusion. FASEB J., 2010, 24(8), 3052-3065.
    • (2010) FASEB J , vol.24 , Issue.8 , pp. 3052-3065
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 128
    • 0032524287 scopus 로고    scopus 로고
    • Activation of phospholipase D by phosphatidic acid. Enhanced vesicle binding.; phosphatidic acid-Ca2+ interaction.; or an allosteric effect?
    • Geng, D.; Chura, J.; and M. F. Roberts. Activation of phospholipase D by phosphatidic acid. Enhanced vesicle binding.; phosphatidic acid-Ca2+ interaction.; or an allosteric effect? J. Biol. Chem., 1998, 273(20), 12195-12202.
    • (1998) J. Biol. Chem , vol.273 , Issue.20 , pp. 12195-12202
    • Geng, D.1    Chura, J.2    Roberts, M.F.3
  • 129
    • 0028030694 scopus 로고
    • Annexin V binding to the outer leaflet of small unilamellar vesicles leads to altered inner-leaflet properties: 31P-and 1H-NMR studies
    • Swairjo, M. A.; Roberts, M. F.; Campos, M. B.; Dedman, J. R.; Seaton, B. A. Annexin V binding to the outer leaflet of small unilamellar vesicles leads to altered inner-leaflet properties: 31P-and 1H-NMR studies. Biochemistry, 1994, 33(36), 10944-10950.
    • (1994) Biochemistry , vol.33 , Issue.36 , pp. 10944-10950
    • Swairjo, M.A.1    Roberts, M.F.2    Campos, M.B.3    Dedman, J.R.4    Seaton, B.A.5
  • 130
    • 0029182774 scopus 로고
    • Does the binding of clusters of basic residues to acidic lipids induce domain formation in membranes?
    • Buser, C. A.; Kim, J.; McLaughlin, S.; Peitzsch, R. M. Does the binding of clusters of basic residues to acidic lipids induce domain formation in membranes? Mol. Membr. Biol., 1995, 12(1), 69-75.
    • (1995) Mol. Membr. Biol , vol.12 , Issue.1 , pp. 69-75
    • Buser, C.A.1    Kim, J.2    McLaughlin, S.3    Peitzsch, R.M.4
  • 131
    • 0029863068 scopus 로고    scopus 로고
    • Rytomaa.; M. and P.K. Kinnunen. Dissociation of cytochrome c from liposomes by histone H1. Comparison with basic peptides. Biochemistry, 1996, 35(14), 4529-4539.
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4529-4539
    • Rytomaa, M.1    Kinnunen, P.K.2
  • 132
    • 0031927361 scopus 로고    scopus 로고
    • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4.;5-bisphosphate: An electrostatic model and experimental results
    • Denisov, G.; Wanaski, S.; Luan, P.; Glaser, M.; McLaughlin, S. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4.;5-bisphosphate: an electrostatic model and experimental results. Biophys. J.; 1998, 74(2 Pt 1), 731-744.
    • (1998) Biophys. J , vol.74 , Issue.2 Pt 1 , pp. 731-744
    • Denisov, G.1    Wanaski, S.2    Luan, P.3    Glaser, M.4    McLaughlin, S.5
  • 133
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • Sun, W.; Yan, Q.; Vida, T. A.; Bean, A. J. Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J. Cell Biol., 2003, 162(1), 125-137.
    • (2003) J. Cell Biol , vol.162 , Issue.1 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 134
    • 2442492169 scopus 로고    scopus 로고
    • Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes
    • Yan, Q.; Sun, W.; McNew, J. A.; Vida, T. A.; Bean, A. J. Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes. J. Biol. Chem., 2004, 279(18), 18270-18276.
    • (2004) J. Biol. Chem , vol.279 , Issue.18 , pp. 18270-18276
    • Yan, Q.1    Sun, W.2    McNew, J.A.3    Vida, T.A.4    Bean, A.J.5
  • 136
    • 84858145258 scopus 로고    scopus 로고
    • Annexin A5 stimulates autophagy and inhibits endocytosis
    • Ghislat, G.; C. Aguado, and E. Knecht. Annexin A5 stimulates autophagy and inhibits endocytosis. J. Cell Sci., 2012, 125(Pt 1), 92-107.
    • (2012) J. Cell Sci , vol.125 , Issue.Pt 1 , pp. 92-107
    • Ghislat, G.1    Aguado, C.2    Knecht, E.3
  • 137
    • 84869828593 scopus 로고    scopus 로고
    • New Ca2+-dependent regulators of autophagosome maturation
    • Ghislat, G. and E. Knecht. New Ca2+-dependent regulators of autophagosome maturation. Commun. Integr. Biol., 2012, 5(4).
    • (2012) Commun. Integr. Biol , vol.5 , Issue.4
    • Ghislat, G.1    Knecht, E.2
  • 139
    • 0034208540 scopus 로고    scopus 로고
    • Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells
    • Huber, L.A.; Fialka, I.; Paiha, K.; Hunziker, W.; Sacks, D. B.; Bähler, M.; Way, M.; Gagescu, R.; Gruenberg, J. Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells. Traffic, 2000, 1(6), 494-503.
    • (2000) Traffic , vol.1 , Issue.6 , pp. 494-503
    • Huber, L.A.1    Fialka, I.2    Paiha, K.3    Hunziker, W.4    Sacks, D.B.5    Bähler, M.6    Way, M.7    Gagescu, R.8    Gruenberg, J.9
  • 140
    • 0344875996 scopus 로고    scopus 로고
    • Calmodulin-dependent regulation of a lipid binding domain in the v-SNARE synaptobrevin and its role in vesicular fusion
    • De Haro, L.; Quetglas, S.; Iborra, C.; Lévêque, C.; Seagar, M. Calmodulin-dependent regulation of a lipid binding domain in the v-SNARE synaptobrevin and its role in vesicular fusion. Biol. Cell, 2003, 95(7), 459-464.
    • (2003) Biol. Cell , vol.95 , Issue.7 , pp. 459-464
    • de Haro, L.1    Quetglas, S.2    Iborra, C.3    Lévêque, C.4    Seagar, M.5
  • 141
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium-and phospholipid-binding proteins
    • Raynal, P. and H.B. Pollard. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium-and phospholipid-binding proteins. Biochim. Biophys. Acta., 1994, 1197(1), 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , Issue.1 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 143
    • 34447543021 scopus 로고    scopus 로고
    • Annexins and endocytosis
    • Futter, C.E. and I.J. White. Annexins and endocytosis. Traffic, 2007, 8(8), 951-8
    • (2007) Traffic , vol.8 , Issue.8 , pp. 951-958
    • Futter, C.E.1    White, I.J.2


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