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Volumn 4 OCT, Issue , 2013, Pages

Calcium-permeable ion channels in control of autophagy and cancer

Author keywords

Autophagy; Calcium; Cancer; Ion channels; TRP

Indexed keywords

BECLIN 1; CALCIUM CHANNEL L TYPE; CALCIUM ION; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; DEATH ASSOCIATED PROTEIN KINASE; TRANSIENT RECEPTOR POTENTIAL CHANNEL M1; TRANSIENT RECEPTOR POTENTIAL CHANNEL M2; TRANSIENT RECEPTOR POTENTIAL CHANNEL M3; VANILLOID RECEPTOR 1;

EID: 84885348627     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2013.00272     Document Type: Article
Times cited : (100)

References (148)
  • 1
    • 84864003589 scopus 로고    scopus 로고
    • Growth inhibition by miR-519 via multiple p21-inducing pathways
    • doi:10.1128/MCB.00510-12
    • Abdelmohsen, K., Srikantan, S., Tominaga, K., Kang, M. J., Yaniv, Y., Martindale, J. L., et al. (2012). Growth inhibition by miR-519 via multiple p21-inducing pathways. Mol. Cell. Biol. 32, 2530-2548. doi:10.1128/MCB.00510-12.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2530-2548
    • Abdelmohsen, K.1    Srikantan, S.2    Tominaga, K.3    Kang, M.J.4    Yaniv, Y.5    Martindale, J.L.6
  • 2
    • 0037072286 scopus 로고    scopus 로고
    • The neurogenetics of mucolipidosis type IV
    • doi:10.1212/WNL.59.3.306
    • Altarescu, G., Sun, M., Moore, D. F., Smith, J. A., Wiggs, E. A., Solomon, B. I., et al. (2002). The neurogenetics of mucolipidosis type IV. Neurology 59, 306-313. doi:10.1212/WNL.59.3.306.
    • (2002) Neurology , vol.59 , pp. 306-313
    • Altarescu, G.1    Sun, M.2    Moore, D.F.3    Smith, J.A.4    Wiggs, E.A.5    Solomon, B.I.6
  • 3
    • 79951847989 scopus 로고    scopus 로고
    • Principles and current strategies for targeting autophagy for cancer treatment
    • doi:10.1158/1078-0432.CCR-10-2634
    • Amaravadi, R. K., Lippincott-Schwartz, J., Yin, X. M., Weiss, W. A., Takebe, N., Timmer, W., et al. (2011). Principles and current strategies for targeting autophagy for cancer treatment. Clin. Cancer Res. 17, 654-666. doi:10.1158/1078-0432.CCR-10-2634.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 654-666
    • Amaravadi, R.K.1    Lippincott-Schwartz, J.2    Yin, X.M.3    Weiss, W.A.4    Takebe, N.5    Timmer, W.6
  • 4
    • 33846794896 scopus 로고    scopus 로고
    • Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma
    • doi:10.1172/JCI28833
    • Amaravadi, R. K., Yu, D., Lum, J. J., Bui, T., Christophorou, M. A., Evan, G. I., et al. (2007). Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma. J. Clin. Invest. 117, 326-336. doi:10.1172/JCI28833.
    • (2007) J. Clin. Invest. , vol.117 , pp. 326-336
    • Amaravadi, R.K.1    Yu, D.2    Lum, J.J.3    Bui, T.4    Christophorou, M.A.5    Evan, G.I.6
  • 5
    • 78649536834 scopus 로고    scopus 로고
    • Insulin/phosphoinositide 3-kinase pathway accelerates the glucose-induced first-phase insulin secretion through TrpV2 recruitment in pancreatic beta-cells
    • doi:10.1042/BJ20100864
    • Aoyagi, K., Ohara-Imaizumi, M., Nishiwaki, C., Nakamichi, Y., and Nagamatsu, S. (2010). Insulin/phosphoinositide 3-kinase pathway accelerates the glucose-induced first-phase insulin secretion through TrpV2 recruitment in pancreatic beta-cells. Biochem. J. 432, 375-386. doi:10.1042/BJ20100864.
    • (2010) Biochem. J. , vol.432 , pp. 375-386
    • Aoyagi, K.1    Ohara-Imaizumi, M.2    Nishiwaki, C.3    Nakamichi, Y.4    Nagamatsu, S.5
  • 6
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • doi:10.1074/jbc. C100319200
    • Arico, S., Petiot, A., Bauvy, C., Dubbelhuis, P. F., Meijer, A. J., Codogno, P., et al. (2001). The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. 276, 35243-35246. doi:10.1074/jbc. C100319200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35243-35246
    • Arico, S.1    Petiot, A.2    Bauvy, C.3    Dubbelhuis, P.F.4    Meijer, A.J.5    Codogno, P.6
  • 7
    • 0034894817 scopus 로고    scopus 로고
    • Mucolipidosis type IV
    • doi:10.1006/mgme.2001.3195
    • Bach, G. (2001). Mucolipidosis type IV. Mol. Genet. Metab. 73, 197-203. doi:10.1006/mgme.2001.3195.
    • (2001) Mol. Genet. Metab. , vol.73 , pp. 197-203
    • Bach, G.1
  • 8
    • 80051946060 scopus 로고    scopus 로고
    • Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
    • doi:10.1038/nature10234
    • Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M., Belcher-Timme, C. A., Sancak, Y., et al. (2011). Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 476, 341-345. doi:10.1038/nature10234.
    • (2011) Nature , vol.476 , pp. 341-345
    • Baughman, J.M.1    Perocchi, F.2    Girgis, H.S.3    Plovanich, M.4    Belcher-Timme, C.A.5    Sancak, Y.6
  • 9
    • 34447542435 scopus 로고    scopus 로고
    • The menthol receptor TRPM8 is the principal detector of environmental cold
    • doi:10.1038/nature05910
    • Bautista, D. M., Siemens, J., Glazer, J. M., Tsuruda, P. R., Basbaum, A. I., Stucky, C. L., et al. (2007). The menthol receptor TRPM8 is the principal detector of environmental cold. Nature 448, 204-208. doi:10.1038/nature05910.
    • (2007) Nature , vol.448 , pp. 204-208
    • Bautista, D.M.1    Siemens, J.2    Glazer, J.M.3    Tsuruda, P.R.4    Basbaum, A.I.5    Stucky, C.L.6
  • 10
    • 84883776628 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore:a mystery solved
    • doi:10.3389/fphys.2013.00095
    • Bernardi, P. (2013). The mitochondrial permeability transition pore:a mystery solved. Front. Physiol. 4:95. doi:10.3389/fphys.2013.00095.
    • (2013) Front. Physiol. , vol.4 , pp. 95
    • Bernardi, P.1
  • 11
    • 84863206432 scopus 로고    scopus 로고
    • The permeability transition pore as a Ca(2+) release channel:new answers to an old question
    • doi:10.1016/j.ceca.2012.03.004
    • Bernardi, P., and von Stockum, S. (2012). The permeability transition pore as a Ca(2+) release channel:new answers to an old question. Cell Calcium 52, 22-27. doi:10.1016/j.ceca.2012.03.004.
    • (2012) Cell Calcium , vol.52 , pp. 22-27
    • Bernardi, P.1    von Stockum, S.2
  • 12
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling:dynamics, homeostasis and remodelling
    • doi:10.1038/nrm1155
    • Berridge, M. J., Bootman, M. D., and Roderick, H. L. (2003). Calcium signalling:dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol. 4, 517-529. doi:10.1038/nrm1155.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 13
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • doi:10.1038/35036035
    • Berridge, M. J., Lipp, P., and Bootman, M. D. (2000). The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol. 1, 11-21. doi:10.1038/35036035.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 14
    • 4544252174 scopus 로고    scopus 로고
    • Apoptosis and calcium:new roles for cytochrome c and inositol 1 4, 5-trisphosphate
    • Boehning, D., Patterson, R. L., and Snyder, S. H. (2004). Apoptosis and calcium:new roles for cytochrome c and inositol 1 4, 5-trisphosphate. Cell Cycle 3, 252-254.
    • (2004) Cell Cycle , vol.3 , pp. 252-254
    • Boehning, D.1    Patterson, R.L.2    Snyder, S.H.3
  • 15
  • 16
    • 0036123997 scopus 로고    scopus 로고
    • The ins and outs of polycystin-2 as a calcium release channel
    • doi:10.1038/ncb0302-e56
    • Cahalan, M. D. (2002). The ins and outs of polycystin-2 as a calcium release channel. Nat. Cell Biol. 4, E56-E57. doi:10.1038/ncb0302-e56.
    • (2002) Nat. Cell Biol. , vol.4
    • Cahalan, M.D.1
  • 17
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • doi:10.1038/nature08030
    • Calcraft, P. J., Ruas, M., Pan, Z., Cheng, X., Arredouani, A., Hao, X., et al. (2009). NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 459, 596-600. doi:10.1038/nature08030.
    • (2009) Nature , vol.459 , pp. 596-600
    • Calcraft, P.J.1    Ruas, M.2    Pan, Z.3    Cheng, X.4    Arredouani, A.5    Hao, X.6
  • 18
    • 84863224750 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) signals in autophagy
    • doi:10.1016/j.ceca.2012.03.001
    • Cardenas, C., and Foskett, J. K. (2012). Mitochondrial Ca(2+) signals in autophagy. Cell Calcium 52, 44-51. doi:10.1016/j.ceca.2012.03.001.
    • (2012) Cell Calcium , vol.52 , pp. 44-51
    • Cardenas, C.1    Foskett, J.K.2
  • 19
    • 77955041880 scopus 로고    scopus 로고
    • Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria
    • doi:10.1016/j.cell.2010.06.007
    • Cardenas, C., Miller, R. A., Smith, I., Bui, T., Molgo, J., Muller, M., et al. (2010). Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria. Cell 142, 270-283. doi:10.1016/j.cell.2010.06.007.
    • (2010) Cell , vol.142 , pp. 270-283
    • Cardenas, C.1    Miller, R.A.2    Smith, I.3    Bui, T.4    Molgo, J.5    Muller, M.6
  • 20
    • 77953704724 scopus 로고    scopus 로고
    • Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells
    • doi:10.4161/auto.6.4.11553
    • Carreira, R. S., Lee, Y., Ghochani, M., Gustafsson, A. B., and Gottlieb, R. A. (2010). Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells. Autophagy 6, 462-472. doi:10.4161/auto.6.4.11553.
    • (2010) Autophagy , vol.6 , pp. 462-472
    • Carreira, R.S.1    Lee, Y.2    Ghochani, M.3    Gustafsson, A.B.4    Gottlieb, R.A.5
  • 21
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • doi:10.1038/18906
    • Caterina, M. J., Rosen, T. A., Tominaga, M., Brake, A. J., and Julius, D. (1999). A capsaicin-receptor homologue with a high threshold for noxious heat. Nature 398, 436-441. doi:10.1038/18906.
    • (1999) Nature , vol.398 , pp. 436-441
    • Caterina, M.J.1    Rosen, T.A.2    Tominaga, M.3    Brake, A.J.4    Julius, D.5
  • 22
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor:a heat-activated ion channel in the pain pathway
    • doi:10.1038/39807
    • Caterina, M. J., Schumacher, M. A., Tominaga, M., Rosen, T. A., Levine, J. D., and Julius, D. (1997). The capsaicin receptor:a heat-activated ion channel in the pain pathway. Nature 389, 816-824. doi:10.1038/39807.
    • (1997) Nature , vol.389 , pp. 816-824
    • Caterina, M.J.1    Schumacher, M.A.2    Tominaga, M.3    Rosen, T.A.4    Levine, J.D.5    Julius, D.6
  • 23
    • 79251577061 scopus 로고    scopus 로고
    • The regulation of autophagy-unanswered questions
    • doi:10.1242/jcs.064576
    • Chen, Y., and Klionsky, D. J. (2011). The regulation of autophagy-unanswered questions. J. Cell Sci. 124, 161-170. doi:10.1242/jcs.064576.
    • (2011) J. Cell Sci. , vol.124 , pp. 161-170
    • Chen, Y.1    Klionsky, D.J.2
  • 24
    • 37349067228 scopus 로고    scopus 로고
    • Oxidative stress induces autophagic cell death independent of apoptosis in transformed and cancer cells
    • doi:10.1038/sj.cdd.4402233
    • Chen, Y., McMillan-Ward, E., Kong, J., Israels, S. J., and Gibson, S. B. (2008). Oxidative stress induces autophagic cell death independent of apoptosis in transformed and cancer cells. Cell Death Differ. 15, 171-182. doi:10.1038/sj.cdd.4402233.
    • (2008) Cell Death Differ. , vol.15 , pp. 171-182
    • Chen, Y.1    McMillan-Ward, E.2    Kong, J.3    Israels, S.J.4    Gibson, S.B.5
  • 25
    • 77949696020 scopus 로고    scopus 로고
    • Mucolipins:intracellular TRPML1-3 channels
    • doi:10.1016/j.febslet.2009.12.056
    • Cheng, X., Shen, D., Samie, M., and Xu, H. (2010). Mucolipins:intracellular TRPML1-3 channels. FEBS Lett. 584, 2013-2021. doi:10.1016/j.febslet.2009.12.056.
    • (2010) FEBS Lett. , vol.584 , pp. 2013-2021
    • Cheng, X.1    Shen, D.2    Samie, M.3    Xu, H.4
  • 26
    • 84863661689 scopus 로고    scopus 로고
    • Therapeutic targets in cancer cell metabolism and autophagy
    • doi:10.1038/nbt.2285
    • Cheong, H., Lu, C., Lindsten, T., and Thompson, C. B. (2012). Therapeutic targets in cancer cell metabolism and autophagy. Nat. Biotechnol. 30, 671-678. doi:10.1038/nbt.2285.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 671-678
    • Cheong, H.1    Lu, C.2    Lindsten, T.3    Thompson, C.B.4
  • 27
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • doi:10.1056/NEJMra1205406
    • Choi, A. M., Ryter, S. W., and Levine, B. (2013). Autophagy in human health and disease. N. Engl. J. Med. 368, 651-662. doi:10.1056/NEJMra1205406.
    • (2013) N. Engl. J. Med. , vol.368 , pp. 651-662
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 28
    • 33947304343 scopus 로고    scopus 로고
    • TRPV6 mediates capsaicin-induced apoptosis in gastric cancer cells-Mechanisms behind a possible new "hot" cancer treatment
    • doi:10.1016/j.bbamcr.2007.01.001
    • Chow, J., Norng, M., Zhang, J., and Chai, J. (2007). TRPV6 mediates capsaicin-induced apoptosis in gastric cancer cells-Mechanisms behind a possible new "hot" cancer treatment. Biochim. Biophys. Acta 1773, 565-576. doi:10.1016/j.bbamcr.2007.01.001.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 565-576
    • Chow, J.1    Norng, M.2    Zhang, J.3    Chai, J.4
  • 29
    • 33947730590 scopus 로고    scopus 로고
    • SnapShot:mammalian TRP channels
    • doi:10.1016/j.cell.2007.03.034
    • Clapham, D. E. (2007). SnapShot:mammalian TRP channels. Cell 129, 220.e1-220.e2. doi:10.1016/j.cell.2007.03.034.
    • (2007) Cell , vol.129
    • Clapham, D.E.1
  • 30
    • 34247380330 scopus 로고    scopus 로고
    • Regulation of autophagy by the inositol trisphosphate receptor
    • doi:10.1038/sj.cdd.4402099
    • Criollo, A., Maiuri, M. C., Tasdemir, E., Vitale, I., Fiebig, A. A., Andrews, D., et al. (2007). Regulation of autophagy by the inositol trisphosphate receptor. Cell Death Differ. 14, 1029-1039. doi:10.1038/sj.cdd.4402099.
    • (2007) Cell Death Differ. , vol.14 , pp. 1029-1039
    • Criollo, A.1    Maiuri, M.C.2    Tasdemir, E.3    Vitale, I.4    Fiebig, A.A.5    Andrews, D.6
  • 31
    • 79955075253 scopus 로고    scopus 로고
    • Macroautophagy is defective in mucolipin-1-deficient mouse neurons
    • doi:10.1016/j.nbd.2010.06.010
    • Curcio-Morelli, C., Charles, F. A., Micsenyi, M. C., Cao, Y., Venugopal, B., Browning, M. F., et al. (2010). Macroautophagy is defective in mucolipin-1-deficient mouse neurons. Neurobiol. Dis. 40, 370-377. doi:10.1016/j.nbd.2010.06.010.
    • (2010) Neurobiol. Dis. , vol.40 , pp. 370-377
    • Curcio-Morelli, C.1    Charles, F.A.2    Micsenyi, M.C.3    Cao, Y.4    Venugopal, B.5    Browning, M.F.6
  • 32
    • 84880471564 scopus 로고    scopus 로고
    • Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells
    • doi:10.1016/j.bbrc.2013.04.015
    • Curry, M. C., Peters, A. A., Kenny, P. A., Roberts-Thomson, S. J., and Monteith, G. R. (2013). Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells. Biochem. Biophys. Res. Commun. 434, 695-700. doi:10.1016/j.bbrc.2013.04.015.
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 695-700
    • Curry, M.C.1    Peters, A.A.2    Kenny, P.A.3    Roberts-Thomson, S.J.4    Monteith, G.R.5
  • 33
    • 80052638037 scopus 로고    scopus 로고
    • A dual role for Ca(2+) in autophagy regulation
    • doi:10.1016/j.ceca.2011.04.001
    • Decuypere, J. P., Bultynck, G., and Parys, J. B. (2011a). A dual role for Ca(2+) in autophagy regulation. Cell Calcium 50, 242-250. doi:10.1016/j.ceca.2011.04.001.
    • (2011) Cell Calcium , vol.50 , pp. 242-250
    • Decuypere, J.P.1    Bultynck, G.2    Parys, J.B.3
  • 34
    • 82855169506 scopus 로고    scopus 로고
    • Ins(1 4, 5)P3 receptor-mediated Ca2+ signaling and autophagy induction are interrelated
    • doi:10.4161/auto.7.12.17909
    • Decuypere, J. P., Welkenhuyzen, K., Luyten, T., Ponsaerts, R., Dewaele, M., Molgo, J., et al. (2011b). Ins(1 4, 5)P3 receptor-mediated Ca2+ signaling and autophagy induction are interrelated. Autophagy 7, 1472-1489. doi:10.4161/auto.7.12.17909.
    • (2011) Autophagy , vol.7 , pp. 1472-1489
    • Decuypere, J.P.1    Welkenhuyzen, K.2    Luyten, T.3    Ponsaerts, R.4    Dewaele, M.5    Molgo, J.6
  • 35
    • 33745713171 scopus 로고    scopus 로고
    • Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis
    • doi:10.1016/j.ccr.2006.06.001
    • Degenhardt, K., Mathew, R., Beaudoin, B., Bray, K., Anderson, D., Chen, G., et al. (2006). Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis. Cancer Cell 10, 51-64. doi:10.1016/j.ccr.2006.06.001.
    • (2006) Cancer Cell , vol.10 , pp. 51-64
    • Degenhardt, K.1    Mathew, R.2    Beaudoin, B.3    Bray, K.4    Anderson, D.5    Chen, G.6
  • 37
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • doi:10.1038/nature10230
    • De Stefani, D., Raffaello, A., Teardo, E., Szabo, I., and Rizzuto, R. (2011). A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 476, 336-340. doi:10.1038/nature10230.
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 38
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • doi:10.1038/nature07311
    • Dong, X. P., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., et al. (2008). The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455, 992-996. doi:10.1038/nature07311.
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5    Kurz, T.6
  • 39
    • 77949695459 scopus 로고    scopus 로고
    • TRP channels of intracellular membranes
    • doi:10.1111/j.1471-4159.2010.06626.x
    • Dong, X. P., Wang, X., and Xu, H. (2010). TRP channels of intracellular membranes. J. Neurochem. 113, 313-328. doi:10.1111/j.1471-4159.2010.06626.x.
    • (2010) J. Neurochem. , vol.113 , pp. 313-328
    • Dong, X.P.1    Wang, X.2    Xu, H.3
  • 40
    • 84885355413 scopus 로고    scopus 로고
    • Targeting apoptosis by the remodelling of calcium-transporting proteins in cancerogenesis
    • doi:10.1111/febs.12246. [Epub ahead of print].
    • Dubois, C., Vanden Abeele, F., and Prevarskaya, N. (2013). Targeting apoptosis by the remodelling of calcium-transporting proteins in cancerogenesis. FEBS J. doi:10.1111/febs.12246. [Epub ahead of print].
    • (2013) FEBS J.
    • Dubois, C.1    Vanden Abeele, F.2    Prevarskaya, N.3
  • 41
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • doi:10.1096/fj.01-0206fje
    • Elmore, S. P., Qian, T., Grissom, S. F., and Lemasters, J. J. (2001). The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J. 15, 2286-2287. doi:10.1096/fj.01-0206fje.
    • (2001) FASEB J. , vol.15 , pp. 2286-2287
    • Elmore, S.P.1    Qian, T.2    Grissom, S.F.3    Lemasters, J.J.4
  • 42
    • 84865494019 scopus 로고    scopus 로고
    • Transient receptor potential vanilloid 1 activation induces autophagy in thymocytes through ROS-regulated AMPK and Atg4C pathways
    • doi:10.1189/jlb.0312123
    • Farfariello, V., Amantini, C., and Santoni, G. (2012). Transient receptor potential vanilloid 1 activation induces autophagy in thymocytes through ROS-regulated AMPK and Atg4C pathways. J. Leukoc. Biol. 92, 421-431. doi:10.1189/jlb.0312123.
    • (2012) J. Leukoc. Biol. , vol.92 , pp. 421-431
    • Farfariello, V.1    Amantini, C.2    Santoni, G.3
  • 43
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and mTOR pathways in cells
    • doi:10.1073/pnas.0502857102
    • Feng, Z., Zhang, H., Levine, A. J., and Jin, S. (2005). The coordinate regulation of the p53 and mTOR pathways in cells. Proc. Natl. Acad. Sci. U.S.A. 102, 8204-8209. doi:10.1073/pnas.0502857102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3    Jin, S.4
  • 44
    • 79958284668 scopus 로고    scopus 로고
    • Orai1 contributes to the establishment of an apoptosis-resistant phenotype in prostate cancer cells
    • doi:10.1038/cddis.2010.52
    • Flourakis, M., Lehen'kyi, V., Beck, B., Raphael, M., Vandenberghe, M., Abeele, F. V., et al. (2010). Orai1 contributes to the establishment of an apoptosis-resistant phenotype in prostate cancer cells. Cell Death Dis. 1, e75. doi:10.1038/cddis.2010.52.
    • (2010) Cell Death Dis. , vol.1
    • Flourakis, M.1    Lehen'kyi, V.2    Beck, B.3    Raphael, M.4    Vandenberghe, M.5    Abeele, F.V.6
  • 45
    • 67349262774 scopus 로고    scopus 로고
    • Insights into Ca2+ homeostasis of advanced prostate cancer cells
    • doi:10.1016/j.bbamcr.2009.01.009
    • Flourakis, M., and Prevarskaya, N. (2009). Insights into Ca2+ homeostasis of advanced prostate cancer cells. Biochim. Biophys. Acta 1793, 1105-1109. doi:10.1016/j.bbamcr.2009.01.009.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1105-1109
    • Flourakis, M.1    Prevarskaya, N.2
  • 46
    • 42149166092 scopus 로고    scopus 로고
    • Colorectal cancer risk in Crohn's disease
    • doi:10.3748/wjg.14.1810
    • Freeman, H. J. (2008). Colorectal cancer risk in Crohn's disease. World J. Gastroenterol. 14, 1810-1811. doi:10.3748/wjg.14.1810.
    • (2008) World J. Gastroenterol. , vol.14 , pp. 1810-1811
    • Freeman, H.J.1
  • 47
    • 68149149128 scopus 로고    scopus 로고
    • The acid test:the discovery of two-pore channels (TPCs) as NAADP-gated endolysosomal Ca(2+) release channels
    • doi:10.1007/s00424-009-0682-y
    • Galione, A., Evans, A. M., Ma, J., Parrington, J., Arredouani, A., Cheng, X., et al. (2009). The acid test:the discovery of two-pore channels (TPCs) as NAADP-gated endolysosomal Ca(2+) release channels. Pflugers Arch. 458, 869-876. doi:10.1007/s00424-009-0682-y.
    • (2009) Pflugers Arch. , vol.458 , pp. 869-876
    • Galione, A.1    Evans, A.M.2    Ma, J.3    Parrington, J.4    Arredouani, A.5    Cheng, X.6
  • 48
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • Gao, W., Ding, W. X., Stolz, D. B., and Yin, X. M. (2008). Induction of macroautophagy by exogenously introduced calcium. Autophagy 4, 754-761.
    • (2008) Autophagy , vol.4 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3    Yin, X.M.4
  • 49
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy.'Protein modifications:beyond the usual suspects' review series
    • doi:10.1038/embor.2008.163
    • Geng, J., and Klionsky, D. J. (2008). The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy.'Protein modifications:beyond the usual suspects' review series. EMBO Rep. 9, 859-864. doi:10.1038/embor.2008.163.
    • (2008) EMBO Rep. , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 51
    • 84862907943 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP
    • doi:10.1093/hmg/ddr481
    • Gomez-Suaga, P., Luzon-Toro, B., Churamani, D., Zhang, L., Bloor-Young, D., Patel, S., et al. (2012). Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP. Hum. Mol. Genet. 21, 511-525. doi:10.1093/hmg/ddr481.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 511-525
    • Gomez-Suaga, P.1    Luzon-Toro, B.2    Churamani, D.3    Zhang, L.4    Bloor-Young, D.5    Patel, S.6
  • 52
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • Gordon, P. B., Holen, I., Fosse, M., Rotnes, J. S., and Seglen, P. O. (1993). Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J. Biol. Chem. 268, 26107-26112.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26107-26112
    • Gordon, P.B.1    Holen, I.2    Fosse, M.3    Rotnes, J.S.4    Seglen, P.O.5
  • 53
    • 84856948227 scopus 로고    scopus 로고
    • Impaired autophagy and organellar dysfunction in pancreatitis
    • doi:10.1111/j.1440-1746.2011.07004.x
    • Gukovsky, I., Pandol, S. J., Mareninova, O. A., Shalbueva, N., Jia, W., and Gukovskaya, A. S. (2012). Impaired autophagy and organellar dysfunction in pancreatitis. J. Gastroenterol. Hepatol. 27(Suppl. 2), 27-32. doi:10.1111/j.1440-1746.2011.07004.x.
    • (2012) J. Gastroenterol. Hepatol. , vol.27 , Issue.SUPPL. 2 , pp. 27-32
    • Gukovsky, I.1    Pandol, S.J.2    Mareninova, O.A.3    Shalbueva, N.4    Jia, W.5    Gukovskaya, A.S.6
  • 54
    • 42649112409 scopus 로고    scopus 로고
    • Amino acids activate mTOR complex 1 via Ca2+/CaM signaling to hVps34
    • doi:10.1016/j.cmet.2008.03.002
    • Gulati, P., Gaspers, L. D., Dann, S. G., Joaquin, M., Nobukuni, T., Natt, F., et al. (2008). Amino acids activate mTOR complex 1 via Ca2+/CaM signaling to hVps34. Cell Metab. 7, 456-465. doi:10.1016/j.cmet.2008.03.002.
    • (2008) Cell Metab. , vol.7 , pp. 456-465
    • Gulati, P.1    Gaspers, L.D.2    Dann, S.G.3    Joaquin, M.4    Nobukuni, T.5    Natt, F.6
  • 55
    • 84859609587 scopus 로고    scopus 로고
    • Targeting autophagy potentiates chemotherapy-induced apoptosis and proliferation inhibition in hepatocarcinoma cells
    • doi:10.1016/j.canlet.2012.03.002
    • Guo, X. L., Li, D., Hu, F., Song, J. R., Zhang, S. S., Deng, W. J., et al. (2012). Targeting autophagy potentiates chemotherapy-induced apoptosis and proliferation inhibition in hepatocarcinoma cells. Cancer Lett. 320, 171-179. doi:10.1016/j.canlet.2012.03.002.
    • (2012) Cancer Lett. , vol.320 , pp. 171-179
    • Guo, X.L.1    Li, D.2    Hu, F.3    Song, J.R.4    Zhang, S.S.5    Deng, W.J.6
  • 56
    • 27744530243 scopus 로고    scopus 로고
    • Capsaicin differentially modulates voltage-activated calcium channel currents in dorsal root ganglion neurones of rats
    • doi:10.1016/j.brainres.2005.09.033
    • Hagenacker, T., Splettstoesser, F., Greffrath, W., Treede, R. D., and Busselberg, D. (2005). Capsaicin differentially modulates voltage-activated calcium channel currents in dorsal root ganglion neurones of rats. Brain Res. 1062, 74-85. doi:10.1016/j.brainres.2005.09.033.
    • (2005) Brain Res. , vol.1062 , pp. 74-85
    • Hagenacker, T.1    Splettstoesser, F.2    Greffrath, W.3    Treede, R.D.4    Busselberg, D.5
  • 57
    • 0034525627 scopus 로고    scopus 로고
    • Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals
    • doi:10.1054/ceca.2000.0169
    • Hajnoczky, G., Csordas, G., Madesh, M., and Pacher, P. (2000). Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals. Cell Calcium 28, 349-363. doi:10.1054/ceca.2000.0169.
    • (2000) Cell Calcium , vol.28 , pp. 349-363
    • Hajnoczky, G.1    Csordas, G.2    Madesh, M.3    Pacher, P.4
  • 58
    • 0034700483 scopus 로고    scopus 로고
    • Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents
    • doi:10.1038/35050128
    • Hanaoka, K., Qian, F., Boletta, A., Bhunia, A. K., Piontek, K., Tsiokas, L., et al. (2000). Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents. Nature 408, 990-994. doi:10.1038/35050128.
    • (2000) Nature , vol.408 , pp. 990-994
    • Hanaoka, K.1    Qian, F.2    Boletta, A.3    Bhunia, A.K.4    Piontek, K.5    Tsiokas, L.6
  • 59
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • doi:10.1016/j.ceb.2010.01.001
    • He, C., and Levine, B. (2010). The Beclin 1 interactome. Curr. Opin. Cell Biol. 22, 140-149. doi:10.1016/j.ceb.2010.01.001.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 140-149
    • He, C.1    Levine, B.2
  • 60
    • 34447093424 scopus 로고    scopus 로고
    • Role of STIM and Orai proteins in the store-operated calcium signaling pathway
    • doi:10.1016/j.ceca.2007.03.009
    • Hewavitharana, T., Deng, X., Soboloff, J., and Gill, D. L. (2007). Role of STIM and Orai proteins in the store-operated calcium signaling pathway. Cell Calcium 42, 173-182. doi:10.1016/j.ceca.2007.03.009.
    • (2007) Cell Calcium , vol.42 , pp. 173-182
    • Hewavitharana, T.1    Deng, X.2    Soboloff, J.3    Gill, D.L.4
  • 61
    • 33846189759 scopus 로고    scopus 로고
    • Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2
    • doi:10.1016/j.molcel.2006.12.009
    • Hoyer-Hansen, M., Bastholm, L., Szyniarowski, P., Campanella, M., Szabadkai, G., Farkas, T., et al. (2007). Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2. Mol. Cell 25, 193-205. doi:10.1016/j.molcel.2006.12.009.
    • (2007) Mol. Cell , vol.25 , pp. 193-205
    • Hoyer-Hansen, M.1    Bastholm, L.2    Szyniarowski, P.3    Campanella, M.4    Szabadkai, G.5    Farkas, T.6
  • 62
    • 66349103732 scopus 로고    scopus 로고
    • Cathepsin L mediates resveratrol-induced autophagy and apoptotic cell death in cervical cancer cells
    • doi:10.4161/auto.5.4.7666
    • Hsu, K. F., Wu, C. L., Huang, S. C., Wu, C. M., Hsiao, J. R., Yo, Y. T., et al. (2009). Cathepsin L mediates resveratrol-induced autophagy and apoptotic cell death in cervical cancer cells. Autophagy 5, 451-460. doi:10.4161/auto.5.4.7666.
    • (2009) Autophagy , vol.5 , pp. 451-460
    • Hsu, K.F.1    Wu, C.L.2    Huang, S.C.3    Wu, C.M.4    Hsiao, J.R.5    Yo, Y.T.6
  • 63
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • doi:10.1083/jcb.200109094
    • Inbal, B., Bialik, S., Sabanay, I., Shani, G., and Kimchi, A. (2002). DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J. Cell Biol. 157, 455-468. doi:10.1083/jcb.200109094.
    • (2002) J. Cell Biol. , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 64
    • 21444442926 scopus 로고    scopus 로고
    • Radiation-induced autophagy is associated with LC3 and its inhibition sensitizes malignant glioma cells
    • Ito, H., Daido, S., Kanzawa, T., Kondo, S., and Kondo, Y. (2005). Radiation-induced autophagy is associated with LC3 and its inhibition sensitizes malignant glioma cells. Int. J. Oncol. 26, 1401-1410.
    • (2005) Int. J. Oncol. , vol.26 , pp. 1401-1410
    • Ito, H.1    Daido, S.2    Kanzawa, T.3    Kondo, S.4    Kondo, Y.5
  • 65
    • 33846022005 scopus 로고    scopus 로고
    • Mitochondrial aberrations in mucolipidosis Type, I
    • doi:10.1074/jbc. M607982200
    • Jennings, J. J. Jr., Zhu, J. H., Rbaibi, Y., Luo, X., Chu, C. T., and Kiselyov, K. (2006). Mitochondrial aberrations in mucolipidosis Type, I. V. J. Biol. Chem. 281, 39041-39050. doi:10.1074/jbc. M607982200.
    • (2006) V. J. Biol. Chem. , vol.281 , pp. 39041-39050
    • Jennings Jr., J.J.1    Zhu, J.H.2    Rbaibi, Y.3    Luo, X.4    Chu, C.T.5    Kiselyov, K.6
  • 66
    • 77955463362 scopus 로고    scopus 로고
    • TRPM2 channel properties, functions and therapeutic potentials
    • doi:10.1517/14728222.2010.510135
    • Jiang, L. H., Yang, W., Zou, J., and Beech, D. J. (2010). TRPM2 channel properties, functions and therapeutic potentials. Expert Opin. Ther. Targets 14, 973-988. doi:10.1517/14728222.2010.510135.
    • (2010) Expert Opin. Ther. Targets , vol.14 , pp. 973-988
    • Jiang, L.H.1    Yang, W.2    Zou, J.3    Beech, D.J.4
  • 67
    • 0033162068 scopus 로고    scopus 로고
    • Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I
    • doi:10.1038/11086
    • Kanzaki, M., Zhang, Y. Q., Mashima, H., Li, L., Shibata, H., and Kojima, I. (1999). Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I. Nat. Cell Biol. 1, 165-170. doi:10.1038/11086.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 165-170
    • Kanzaki, M.1    Zhang, Y.Q.2    Mashima, H.3    Li, L.4    Shibata, H.5    Kojima, I.6
  • 68
    • 77952759763 scopus 로고    scopus 로고
    • Role of inositol trisphosphate receptors in autophagy in DT40 cells
    • doi:10.1074/jbc. M110.114207
    • Khan, M. T., and Joseph, S. K. (2010). Role of inositol trisphosphate receptors in autophagy in DT40 cells. J. Biol. Chem. 285, 16912-16920. doi:10.1074/jbc. M110.114207.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16912-16920
    • Khan, M.T.1    Joseph, S.K.2
  • 69
    • 67649870315 scopus 로고    scopus 로고
    • The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy
    • doi:10.1111/j.1600-0854.2009.00924.x
    • Kim, H. J., Soyombo, A. A., Tjon-Kon-Sang, S., So, I., and Muallem, S. (2009). The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy. Traffic 10, 1157-1167. doi:10.1111/j.1600-0854.2009.00924.x.
    • (2009) Traffic , vol.10 , pp. 1157-1167
    • Kim, H.J.1    Soyombo, A.A.2    Tjon-Kon-Sang, S.3    So, I.4    Muallem, S.5
  • 70
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • doi:10.1038/ncb2152
    • Kim, J., Kundu, M., Viollet, B., and Guan, K. L. (2011). AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13, 132-141. doi:10.1038/ncb2152.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 71
    • 84871940714 scopus 로고    scopus 로고
    • Chloroquine in cancer therapy:a double-edged sword of autophagy
    • doi:10.1158/0008-5472.CAN-12-2464
    • Kimura, T., Takabatake, Y., Takahashi, A., and Isaka, Y. (2013). Chloroquine in cancer therapy:a double-edged sword of autophagy. Cancer Res. 73, 3-7. doi:10.1158/0008-5472.CAN-12-2464.
    • (2013) Cancer Res. , vol.73 , pp. 3-7
    • Kimura, T.1    Takabatake, Y.2    Takahashi, A.3    Isaka, Y.4
  • 72
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy:unanswered questions
    • doi:10.1242/jcs.01620
    • Klionsky, D. J. (2005). The molecular machinery of autophagy:unanswered questions. J. Cell Sci. 118, 7-18. doi:10.1242/jcs.01620.
    • (2005) J. Cell Sci. , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 73
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • doi:10.4161/auto.19496
    • Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., et al. (2012). Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8, 445-544. doi:10.4161/auto.19496.
    • (2012) Autophagy , vol.8 , pp. 445-544
    • Klionsky, D.J.1    Abdalla, F.C.2    Abeliovich, H.3    Abraham, R.T.4    Acevedo-Arozena, A.5    Adeli, K.6
  • 74
    • 77950637041 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha (TNF-alpha) enhances functional thermal and chemical responses of TRP cation channels in human synoviocytes
    • doi:10.1186/1744-8069-5-49
    • Kochukov, M. Y., McNearney, T. A., Yin, H., Zhang, L., Ma, F., Ponomareva, L., et al. (2009). Tumor necrosis factor-alpha (TNF-alpha) enhances functional thermal and chemical responses of TRP cation channels in human synoviocytes. Mol. Pain 5, 49. doi:10.1186/1744-8069-5-49.
    • (2009) Mol. Pain , vol.5 , pp. 49
    • Kochukov, M.Y.1    McNearney, T.A.2    Yin, H.3    Zhang, L.4    Ma, F.5    Ponomareva, L.6
  • 75
    • 25444440875 scopus 로고    scopus 로고
    • The role of autophagy in cancer development and response to therapy
    • doi:10.1038/nrc1692
    • Kondo, Y., Kanzawa, T., Sawaya, R., and Kondo, S. (2005). The role of autophagy in cancer development and response to therapy. Nat. Rev. Cancer 5, 726-734. doi:10.1038/nrc1692.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 726-734
    • Kondo, Y.1    Kanzawa, T.2    Sawaya, R.3    Kondo, S.4
  • 76
    • 0036122434 scopus 로고    scopus 로고
    • Polycystin-2 is an intracellular calcium release channel
    • doi:10.1038/ncb754
    • Koulen, P., Cai, Y., Geng, L., Maeda, Y., Nishimura, S., Witzgall, R., et al. (2002). Polycystin-2 is an intracellular calcium release channel. Nat. Cell Biol. 4, 191-197. doi:10.1038/ncb754.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 191-197
    • Koulen, P.1    Cai, Y.2    Geng, L.3    Maeda, Y.4    Nishimura, S.5    Witzgall, R.6
  • 77
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • doi:10.1016/j.molcel.2010.09.023
    • Kroemer, G., Marino, G., and Levine, B. (2010). Autophagy and the integrated stress response. Mol. Cell 40, 280-293. doi:10.1016/j.molcel.2010.09.023.
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 78
    • 39449105425 scopus 로고    scopus 로고
    • The inositol 1 4, 5-trisphosphate receptor is required to signal autophagic cell death
    • doi:10.1091/mbc. E07-08-0823
    • Lam, D., Kosta, A., Luciani, M. F., and Golstein, P. (2008). The inositol 1 4, 5-trisphosphate receptor is required to signal autophagic cell death. Mol. Biol. Cell 19, 691-700. doi:10.1091/mbc. E07-08-0823.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 691-700
    • Lam, D.1    Kosta, A.2    Luciani, M.F.3    Golstein, P.4
  • 79
    • 84880861312 scopus 로고    scopus 로고
    • Dual inhibition of autophagy and the AKT pathway in prostate cancer
    • doi:10.4161/auto.24921
    • Lamoureux, F., and Zoubeidi, A. (2013). Dual inhibition of autophagy and the AKT pathway in prostate cancer. Autophagy 9, 1119-1120. doi:10.4161/auto.24921.
    • (2013) Autophagy , vol.9 , pp. 1119-1120
    • Lamoureux, F.1    Zoubeidi, A.2
  • 80
    • 70350517076 scopus 로고    scopus 로고
    • TRPM2 functions as a lysosomal Ca2+-release channel in beta cells
    • doi:10.1126/scisignal.2000278
    • Lange, I., Yamamoto, S., Partida-Sanchez, S., Mori, Y., Fleig, A., and Penner, R. (2009). TRPM2 functions as a lysosomal Ca2+-release channel in beta cells. Sci. Signal. 2, ra23. doi:10.1126/scisignal.2000278.
    • (2009) Sci. Signal. , vol.2
    • Lange, I.1    Yamamoto, S.2    Partida-Sanchez, S.3    Mori, Y.4    Fleig, A.5    Penner, R.6
  • 81
    • 1642462152 scopus 로고    scopus 로고
    • Quantitation of the lysosomotropic character of cationic amphiphilic drugs using the fluorescent basic amine Red DND-99
    • doi:10.1016/j.ab.2004.01.010
    • Lemieux, B., Percival, M. D., and Falgueyret, J. P. (2004). Quantitation of the lysosomotropic character of cationic amphiphilic drugs using the fluorescent basic amine Red DND-99. Anal. Biochem. 327, 247-251. doi:10.1016/j.ab.2004.01.010.
    • (2004) Anal. Biochem. , vol.327 , pp. 247-251
    • Lemieux, B.1    Percival, M.D.2    Falgueyret, J.P.3
  • 82
    • 77953289524 scopus 로고    scopus 로고
    • Inhibition of autophagy augments 5-fluorouracil chemotherapy in human colon cancer in vitro and in vivo model
    • doi:10.1016/j.ejca.2010.02.021
    • Li, J., Hou, N., Faried, A., Tsutsumi, S., and Kuwano, H. (2010). Inhibition of autophagy augments 5-fluorouracil chemotherapy in human colon cancer in vitro and in vivo model. Eur. J. Cancer 46, 1900-1909. doi:10.1016/j.ejca.2010.02.021.
    • (2010) Eur. J. Cancer , vol.46 , pp. 1900-1909
    • Li, J.1    Hou, N.2    Faried, A.3    Tsutsumi, S.4    Kuwano, H.5
  • 83
    • 33846204370 scopus 로고    scopus 로고
    • UVRAG:a new player in autophagy and tumor cell growth
    • Liang, C., Feng, P., Ku, B., Oh, B. H., and Jung, J. U. (2007a). UVRAG:a new player in autophagy and tumor cell growth. Autophagy 3, 69-71.
    • (2007) Autophagy , vol.3 , pp. 69-71
    • Liang, C.1    Feng, P.2    Ku, B.3    Oh, B.H.4    Jung, J.U.5
  • 84
    • 33947250696 scopus 로고    scopus 로고
    • The energy sensing LKB1-AMPK pathway regulates p27(kip1) phosphorylation mediating the decision to enter autophagy or apoptosis
    • doi:10.1038/ncb1537
    • Liang, J., Shao, S. H., Xu, Z. X., Hennessy, B., Ding, Z., Larrea, M., et al. (2007b). The energy sensing LKB1-AMPK pathway regulates p27(kip1) phosphorylation mediating the decision to enter autophagy or apoptosis. Nat. Cell Biol. 9, 218-224. doi:10.1038/ncb1537.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 218-224
    • Liang, J.1    Shao, S.H.2    Xu, Z.X.3    Hennessy, B.4    Ding, Z.5    Larrea, M.6
  • 85
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • doi:10.1038/45257
    • Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., et al. (1999). Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 402, 672-676. doi:10.1038/45257.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3    Brown, K.4    Kempkes, B.5    Hibshoosh, H.6
  • 86
    • 84870621600 scopus 로고    scopus 로고
    • MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism
    • doi:10.1038/ncb2622
    • Mallilankaraman, K., Cardenas, C., Doonan, P. J., Chandramoorthy, H. C., Irrinki, K. M., Golenar, T., et al. (2012). MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism. Nat. Cell Biol. 14, 1336-1343. doi:10.1038/ncb2622.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1336-1343
    • Mallilankaraman, K.1    Cardenas, C.2    Doonan, P.J.3    Chandramoorthy, H.C.4    Irrinki, K.M.5    Golenar, T.6
  • 87
    • 47949096781 scopus 로고    scopus 로고
    • Cancer-related inflammation
    • doi:10.1038/nature07205
    • Mantovani, A., Allavena, P., Sica, A., and Balkwill, F. (2008). Cancer-related inflammation. Nature 454, 436-444. doi:10.1038/nature07205.
    • (2008) Nature , vol.454 , pp. 436-444
    • Mantovani, A.1    Allavena, P.2    Sica, A.3    Balkwill, F.4
  • 88
    • 34547132328 scopus 로고    scopus 로고
    • Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3
    • doi:10.1074/jbc. M701194200
    • Marino, G., Salvador-Montoliu, N., Fueyo, A., Knecht, E., Mizushima, N., and Lopez-Otin, C. (2007). Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3. J. Biol. Chem. 282, 18573-18583. doi:10.1074/jbc. M701194200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18573-18583
    • Marino, G.1    Salvador-Montoliu, N.2    Fueyo, A.3    Knecht, E.4    Mizushima, N.5    Lopez-Otin, C.6
  • 89
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • doi:10.1016/j.ceb.2009.12.004
    • Mizushima, N. (2010). The role of the Atg1/ULK1 complex in autophagy regulation. Curr. Opin. Cell Biol. 22, 132-139. doi:10.1016/j.ceb.2009.12.004.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 90
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • doi:10.1038/nature06639
    • Mizushima, N., Levine, B., Cuervo, A. M., and Klionsky, D. J. (2008). Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075. doi:10.1038/nature06639.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 91
    • 76249107718 scopus 로고    scopus 로고
    • Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance
    • doi:10.1158/0008-5472.CAN-09-2205
    • Monet, M., Lehen'kyi, V., Gackiere, F., Firlej, V., Vandenberghe, M., Roudbaraki, M., et al. (2010). Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance. Cancer Res. 70, 1225-1235. doi:10.1158/0008-5472.CAN-09-2205.
    • (2010) Cancer Res. , vol.70 , pp. 1225-1235
    • Monet, M.1    Lehen'kyi, V.2    Gackiere, F.3    Firlej, V.4    Vandenberghe, M.5    Roudbaraki, M.6
  • 92
    • 84866367672 scopus 로고    scopus 로고
    • Calcium channels and pumps in cancer:changes and consequences
    • doi:10.1074/jbc. R112.343061
    • Monteith, G. R., Davis, F. M., and Roberts-Thomson, S. J. (2012). Calcium channels and pumps in cancer:changes and consequences. J. Biol. Chem. 287, 31666-31673. doi:10.1074/jbc. R112.343061.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31666-31673
    • Monteith, G.R.1    Davis, F.M.2    Roberts-Thomson, S.J.3
  • 94
    • 33645533257 scopus 로고    scopus 로고
    • Capsaicin, a component of red peppers, inhibits the growth of androgen-independent, p53 mutant prostate cancer cells
    • doi:10.1158/0008-5472.CAN-05-0087
    • Mori, A., Lehmann, S., O'kelly, J., Kumagai, T., Desmond, J. C., Pervan, M., et al. (2006). Capsaicin, a component of red peppers, inhibits the growth of androgen-independent, p53 mutant prostate cancer cells. Cancer Res. 66, 3222-3229. doi:10.1158/0008-5472.CAN-05-0087.
    • (2006) Cancer Res. , vol.66 , pp. 3222-3229
    • Mori, A.1    Lehmann, S.2    O'kelly, J.3    Kumagai, T.4    Desmond, J.C.5    Pervan, M.6
  • 95
    • 0242266967 scopus 로고    scopus 로고
    • TRPV2 is a component of osmotically sensitive cation channels in murine aortic myocytes
    • doi:10.1161/01.RES.0000097263.10220.0C
    • Muraki, K., Iwata, Y., Katanosaka, Y., Ito, T., Ohya, S., Shigekawa, M., et al. (2003). TRPV2 is a component of osmotically sensitive cation channels in murine aortic myocytes. Circ. Res. 93, 829-838. doi:10.1161/01.RES.0000097263.10220.0C.
    • (2003) Circ. Res. , vol.93 , pp. 829-838
    • Muraki, K.1    Iwata, Y.2    Katanosaka, Y.3    Ito, T.4    Ohya, S.5    Shigekawa, M.6
  • 97
    • 34547521545 scopus 로고    scopus 로고
    • TRP channels in disease
    • doi:10.1016/j.bbadis.2007.02.002
    • Nilius, B. (2007). TRP channels in disease. Biochim. Biophys. Acta 1772, 805-812. doi:10.1016/j.bbadis.2007.02.002.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 805-812
    • Nilius, B.1
  • 98
    • 33846807748 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in disease
    • doi:10.1152/physrev.00021.2006
    • Nilius, B., Owsianik, G., Voets, T., and Peters, J. A. (2007). Transient receptor potential cation channels in disease. Physiol. Rev. 87, 165-217. doi:10.1152/physrev.00021.2006.
    • (2007) Physiol. Rev. , vol.87 , pp. 165-217
    • Nilius, B.1    Owsianik, G.2    Voets, T.3    Peters, J.A.4
  • 99
    • 84864652172 scopus 로고    scopus 로고
    • Role of the inositol 1 4, 5-trisphosphate receptor/Ca2+-release channel in autophagy
    • doi:10.1186/1478-811X-10-17
    • Parys, J. B., Decuypere, J. P., and Bultynck, G. (2012). Role of the inositol 1 4, 5-trisphosphate receptor/Ca2+-release channel in autophagy. Cell Commun. Signal. 10, 17. doi:10.1186/1478-811X-10-17.
    • (2012) Cell Commun. Signal. , vol.10 , pp. 17
    • Parys, J.B.1    Decuypere, J.P.2    Bultynck, G.3
  • 100
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • doi:10.1016/j.cell.2005.07.002
    • Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., et al. (2005). Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122, 927-939. doi:10.1016/j.cell.2005.07.002.
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3    Garuti, R.4    Liang, X.H.5    Mizushima, N.6
  • 101
    • 24644445646 scopus 로고    scopus 로고
    • TRP channels:an overview
    • doi:10.1016/j.ceca.2005.06.028
    • Pedersen, S. F., Owsianik, G., and Nilius, B. (2005). TRP channels:an overview. Cell Calcium 38, 233-252. doi:10.1016/j.ceca.2005.06.028.
    • (2005) Cell Calcium , vol.38 , pp. 233-252
    • Pedersen, S.F.1    Owsianik, G.2    Nilius, B.3
  • 102
    • 0038420824 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1 4, 5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels
    • doi:10.1016/S0143-4160(03)00026-5
    • Peppiatt, C. M., Collins, T. J., Mackenzie, L., Conway, S. J., Holmes, A. B., Bootman, M. D., et al. (2003). 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1 4, 5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels. Cell Calcium 34, 97-108. doi:10.1016/S0143-4160(03)00026-5.
    • (2003) Cell Calcium , vol.34 , pp. 97-108
    • Peppiatt, C.M.1    Collins, T.J.2    Mackenzie, L.3    Conway, S.J.4    Holmes, A.B.5    Bootman, M.D.6
  • 103
    • 80051497127 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP) regulates autophagy in cultured astrocytes
    • doi:10.1074/jbc. C110.216580
    • Pereira, G. J., Hirata, H., Fimia, G. M., Do Carmo, L. G., Bincoletto, C., Han, S. W., et al. (2011). Nicotinic acid adenine dinucleotide phosphate (NAADP) regulates autophagy in cultured astrocytes. J. Biol. Chem. 286, 27875-27881. doi:10.1074/jbc. C110.216580.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27875-27881
    • Pereira, G.J.1    Hirata, H.2    Fimia, G.M.3    Do Carmo, L.G.4    Bincoletto, C.5    Han, S.W.6
  • 104
    • 77949327468 scopus 로고    scopus 로고
    • Ion channels and the hallmarks of cancer
    • doi:10.1016/j.molmed.2010.01.005
    • Prevarskaya, N., Skryma, R., and Shuba, Y. (2010). Ion channels and the hallmarks of cancer. Trends Mol. Med. 16, 107-121. doi:10.1016/j.molmed.2010.01.005.
    • (2010) Trends Mol. Med. , vol.16 , pp. 107-121
    • Prevarskaya, N.1    Skryma, R.2    Shuba, Y.3
  • 105
    • 79960759956 scopus 로고    scopus 로고
    • Calcium in tumour metastasis:new roles for known actors
    • doi:10.1038/nrc3105
    • Prevarskaya, N., Skryma, R., and Shuba, Y. (2011). Calcium in tumour metastasis:new roles for known actors. Nat. Rev. Cancer 11, 609-618. doi:10.1038/nrc3105.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 609-618
    • Prevarskaya, N.1    Skryma, R.2    Shuba, Y.3
  • 106
    • 84879627185 scopus 로고    scopus 로고
    • Mitochondrial calcium uniporter Mcu controls excitotoxicity and is transcriptionally repressed by neuroprotective nuclear calcium signals
    • doi:10.1038/ncomms3034
    • Qiu, J., Tan, Y. W., Hagenston, A. M., Martel, M. A., Kneisel, N., Skehel, P. A., et al. (2013). Mitochondrial calcium uniporter Mcu controls excitotoxicity and is transcriptionally repressed by neuroprotective nuclear calcium signals. Nat. Commun. 4, 2034. doi:10.1038/ncomms3034.
    • (2013) Nat. Commun. , vol.4 , pp. 2034
    • Qiu, J.1    Tan, Y.W.2    Hagenston, A.M.3    Martel, M.A.4    Kneisel, N.5    Skehel, P.A.6
  • 108
    • 78149475088 scopus 로고    scopus 로고
    • Regulation of mammalian autophagy in physiology and pathophysiology
    • doi:10.1152/physrev.00030.2009
    • Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., Garcia-Arencibia, M., Green-Thompson, Z. W., et al. (2010). Regulation of mammalian autophagy in physiology and pathophysiology. Physiol. Rev. 90, 1383-1435. doi:10.1152/physrev.00030.2009.
    • (2010) Physiol. Rev. , vol.90 , pp. 1383-1435
    • Ravikumar, B.1    Sarkar, S.2    Davies, J.E.3    Futter, M.4    Garcia-Arencibia, M.5    Green-Thompson, Z.W.6
  • 109
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • doi:10.1083/jcb.200810098
    • Razi, M., Chan, E. Y., and Tooze, S. A. (2009). Early endosomes and endosomal coatomer are required for autophagy. J. Cell Biol. 185, 305-321. doi:10.1083/jcb.200810098.
    • (2009) J. Cell Biol. , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.2    Tooze, S.A.3
  • 111
    • 84865427488 scopus 로고    scopus 로고
    • Mitochondria as sensors and regulators of calcium signalling
    • doi:10.1038/nrm3412
    • Rizzuto, R., De Stefani, D., Raffaello, A., and Mammucari, C. (2012). Mitochondria as sensors and regulators of calcium signalling. Nat. Rev. Mol. Cell Biol. 13, 566-578. doi:10.1038/nrm3412.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 566-578
    • Rizzuto, R.1    De Stefani, D.2    Raffaello, A.3    Mammucari, C.4
  • 112
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • doi:10.1038/nrd3802
    • Rubinsztein, D. C., Codogno, P., and Levine, B. (2012). Autophagy modulation as a potential therapeutic target for diverse diseases. Nat. Rev. Drug Discov. 11, 709-730. doi:10.1038/nrd3802.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 113
    • 34848916433 scopus 로고    scopus 로고
    • Luminal chloride-dependent activation of endosome calcium channels:patch clamp study of enlarged endosomes
    • doi:10.1074/jbc. M702557200
    • Saito, M., Hanson, P. I., and Schlesinger, P. (2007). Luminal chloride-dependent activation of endosome calcium channels:patch clamp study of enlarged endosomes. J. Biol. Chem. 282, 27327-27333. doi:10.1074/jbc. M702557200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27327-27333
    • Saito, M.1    Hanson, P.I.2    Schlesinger, P.3
  • 114
    • 47249157360 scopus 로고    scopus 로고
    • Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum
    • doi:10.1074/jbc. M710209200
    • Sakaki, K., Wu, J., and Kaufman, R. J. (2008). Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum. J. Biol. Chem. 283, 15370-15380. doi:10.1074/jbc. M710209200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15370-15380
    • Sakaki, K.1    Wu, J.2    Kaufman, R.J.3
  • 115
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • doi:10.1083/jcb.200504035
    • Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., et al. (2005). Lithium induces autophagy by inhibiting inositol monophosphatase. J. Cell Biol. 170, 1101-1111. doi:10.1083/jcb.200504035.
    • (2005) J. Cell Biol. , vol.170 , pp. 1101-1111
    • Sarkar, S.1    Floto, R.A.2    Berger, Z.3    Imarisio, S.4    Cordenier, A.5    Pasco, M.6
  • 116
    • 84878992314 scopus 로고    scopus 로고
    • Autophagy inhibition sensitizes colon cancer cells to antiangiogenic and cytotoxic therapy
    • doi:10.1158/1078-0432.CCR-12-1542
    • Selvakumaran, M., Amaravadi, R. K., Vasilevskaya, I. A., and O'dwyer, P. J. (2013). Autophagy inhibition sensitizes colon cancer cells to antiangiogenic and cytotoxic therapy. Clin. Cancer Res. 19, 2995-3007. doi:10.1158/1078-0432.CCR-12-1542.
    • (2013) Clin. Cancer Res. , vol.19 , pp. 2995-3007
    • Selvakumaran, M.1    Amaravadi, R.K.2    Vasilevskaya, I.A.3    O'dwyer, P.J.4
  • 117
    • 80052338518 scopus 로고    scopus 로고
    • TRP channels in cell survival and cell death in normal and transformed cells
    • doi:10.1016/j.ceca.2011.05.006
    • Shapovalov, G., Lehen'kyi, V., Skryma, R., and Prevarskaya, N. (2011). TRP channels in cell survival and cell death in normal and transformed cells. Cell Calcium 50, 295-302. doi:10.1016/j.ceca.2011.05.006.
    • (2011) Cell Calcium , vol.50 , pp. 295-302
    • Shapovalov, G.1    Lehen'kyi, V.2    Skryma, R.3    Prevarskaya, N.4
  • 118
    • 0033362229 scopus 로고    scopus 로고
    • Mapping of the mucolipidosis type IV gene to chromosome 19p and definition of founder haplotypes
    • doi:10.1086/302549
    • Slaugenhaupt, S. A., Acierno, J. S. Jr., Helbling, L. A., Bove, C., Goldin, E., Bach, G., et al. (1999). Mapping of the mucolipidosis type IV gene to chromosome 19p and definition of founder haplotypes. Am. J. Hum. Genet. 65, 773-778. doi:10.1086/302549.
    • (1999) Am. J. Hum. Genet. , vol.65 , pp. 773-778
    • Slaugenhaupt, S.A.1    Acierno Jr., J.S.2    Helbling, L.A.3    Bove, C.4    Goldin, E.5    Bach, G.6
  • 119
    • 84858336588 scopus 로고    scopus 로고
    • Abeta-induced formation of autophagosomes is mediated by RAGE-CaMKKbeta-AMPK signaling
    • doi:10.1016/j.neurobiolaging.2011.09.039
    • Son, S. M., Jung, E. S., Shin, H. J., Byun, J., and Mook-Jung, I. (2012). Abeta-induced formation of autophagosomes is mediated by RAGE-CaMKKbeta-AMPK signaling. Neurobiol. Aging 33, 1006 e1011-1006 e1023. doi:10.1016/j.neurobiolaging.2011.09.039.
    • (2012) Neurobiol. Aging , vol.33
    • Son, S.M.1    Jung, E.S.2    Shin, H.J.3    Byun, J.4    Mook-Jung, I.5
  • 120
    • 33646344988 scopus 로고    scopus 로고
    • TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity
    • doi:10.1074/jbc. M508211200
    • Soyombo, A. A., Tjon-Kon-Sang, S., Rbaibi, Y., Bashllari, E., Bisceglia, J., Muallem, S., et al. (2006). TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity. J. Biol. Chem. 281, 7294-7301. doi:10.1074/jbc. M508211200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7294-7301
    • Soyombo, A.A.1    Tjon-Kon-Sang, S.2    Rbaibi, Y.3    Bashllari, E.4    Bisceglia, J.5    Muallem, S.6
  • 121
    • 79953153188 scopus 로고    scopus 로고
    • TRPM2:a multifunctional ion channel for calcium signalling
    • doi:10.1113/jphysiol.2010.201855
    • Sumoza-Toledo, A., and Penner, R. (2011). TRPM2:a multifunctional ion channel for calcium signalling. J. Physiol. 589, 1515-1525. doi:10.1113/jphysiol.2010.201855.
    • (2011) J. Physiol. , vol.589 , pp. 1515-1525
    • Sumoza-Toledo, A.1    Penner, R.2
  • 122
    • 34848899280 scopus 로고    scopus 로고
    • Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis
    • doi:10.1038/ncb1634
    • Takahashi, Y., Coppola, D., Matsushita, N., Cualing, H. D., Sun, M., Sato, Y., et al. (2007). Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis. Nat. Cell Biol. 9, 1142-1151. doi:10.1038/ncb1634.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1142-1151
    • Takahashi, Y.1    Coppola, D.2    Matsushita, N.3    Cualing, H.D.4    Sun, M.5    Sato, Y.6
  • 123
    • 79955377420 scopus 로고    scopus 로고
    • Autophagy-deficient mice develop multiple liver tumors
    • doi:10.1101/gad.2016211
    • Takamura, A., Komatsu, M., Hara, T., Sakamoto, A., Kishi, C., Waguri, S., et al. (2011). Autophagy-deficient mice develop multiple liver tumors. Genes Dev. 25, 795-800. doi:10.1101/gad.2016211.
    • (2011) Genes Dev. , vol.25 , pp. 795-800
    • Takamura, A.1    Komatsu, M.2    Hara, T.3    Sakamoto, A.4    Kishi, C.5    Waguri, S.6
  • 124
    • 4344624322 scopus 로고    scopus 로고
    • LC3 conjugation system in mammalian autophagy
    • doi:10.1016/j.biocel.2004.05.009
    • Tanida, I., Ueno, T., and Kominami, E. (2004). LC3 conjugation system in mammalian autophagy. Int. J. Biochem. Cell Biol. 36, 2503-2518. doi:10.1016/j.biocel.2004.05.009.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2503-2518
    • Tanida, I.1    Ueno, T.2    Kominami, E.3
  • 125
    • 28244482299 scopus 로고    scopus 로고
    • Novel role of cold/menthol-sensitive transient receptor potential melastatine family member 8 (TRPM8) in the activation of store-operated channels in LNCaP human prostate cancer epithelial cells
    • doi:10.1074/jbc. M503544200
    • Thebault, S., Lemonnier, L., Bidaux, G., Flourakis, M., Bavencoffe, A., Gordienko, D., et al. (2005). Novel role of cold/menthol-sensitive transient receptor potential melastatine family member 8 (TRPM8) in the activation of store-operated channels in LNCaP human prostate cancer epithelial cells. J. Biol. Chem. 280, 39423-39435. doi:10.1074/jbc. M503544200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39423-39435
    • Thebault, S.1    Lemonnier, L.2    Bidaux, G.3    Flourakis, M.4    Bavencoffe, A.5    Gordienko, D.6
  • 126
    • 78650871500 scopus 로고    scopus 로고
    • Sub-cellular distribution and translocation of TRP channels
    • Toro, C. A., Arias, L. A., and Brauchi, S. (2011). Sub-cellular distribution and translocation of TRP channels. Curr. Pharm. Biotechnol. 12, 12-23.
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 12-23
    • Toro, C.A.1    Arias, L.A.2    Brauchi, S.3
  • 127
    • 0035328671 scopus 로고    scopus 로고
    • Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins
    • Tsavaler, L., Shapero, M. H., Morkowski, S., and Laus, R. (2001). Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins. Cancer Res. 61, 3760-3769.
    • (2001) Cancer Res. , vol.61 , pp. 3760-3769
    • Tsavaler, L.1    Shapero, M.H.2    Morkowski, S.3    Laus, R.4
  • 128
    • 0038414614 scopus 로고    scopus 로고
    • Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity
    • doi:10.1042/BJ20021381
    • Turner, H., Fleig, A., Stokes, A., Kinet, J. P., and Penner, R. (2003). Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity. Biochem. J. 371, 341-350. doi:10.1042/BJ20021381.
    • (2003) Biochem. J. , vol.371 , pp. 341-350
    • Turner, H.1    Fleig, A.2    Stokes, A.3    Kinet, J.P.4    Penner, R.5
  • 129
    • 84872185360 scopus 로고    scopus 로고
    • Feast or famine:role of TRPML in preventing cellular amino acid starvation
    • doi:10.4161/auto.22260
    • Venkatachalam, K., Wong, C. O., and Montell, C. (2013). Feast or famine:role of TRPML in preventing cellular amino acid starvation. Autophagy 9, 98-100. doi:10.4161/auto.22260.
    • (2013) Autophagy , vol.9 , pp. 98-100
    • Venkatachalam, K.1    Wong, C.O.2    Montell, C.3
  • 131
    • 49649089300 scopus 로고    scopus 로고
    • Autophagic dysfunction in mucolipidosis type IV patients
    • doi:10.1093/hmg/ddn174
    • Vergarajauregui, S., Connelly, P. S., Daniels, M. P., and Puertollano, R. (2008). Autophagic dysfunction in mucolipidosis type IV patients. Hum. Mol. Genet. 17, 2723-2737. doi:10.1093/hmg/ddn174.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2723-2737
    • Vergarajauregui, S.1    Connelly, P.S.2    Daniels, M.P.3    Puertollano, R.4
  • 132
    • 67549135655 scopus 로고    scopus 로고
    • The inositol 1 4, 5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1
    • doi:10.1038/cdd.2009.34
    • Vicencio, J. M., Ortiz, C., Criollo, A., Jones, A. W., Kepp, O., Galluzzi, L., et al. (2009). The inositol 1 4, 5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1. Cell Death Differ. 16, 1006-1017. doi:10.1038/cdd.2009.34.
    • (2009) Cell Death Differ. , vol.16 , pp. 1006-1017
    • Vicencio, J.M.1    Ortiz, C.2    Criollo, A.3    Jones, A.W.4    Kepp, O.5    Galluzzi, L.6
  • 133
    • 56549125810 scopus 로고    scopus 로고
    • Cadmium-induced autophagy and apoptosis are mediated by a calcium signaling pathway
    • doi:10.1007/s00018-008-8383-9
    • Wang, S. H., Shih, Y. L., Ko, W. C., Wei, Y. H., and Shih, C. M. (2008). Cadmium-induced autophagy and apoptosis are mediated by a calcium signaling pathway. Cell. Mol. Life Sci. 65, 3640-3652. doi:10.1007/s00018-008-8383-9.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3640-3652
    • Wang, S.H.1    Shih, Y.L.2    Ko, W.C.3    Wei, Y.H.4    Shih, C.M.5
  • 134
    • 84861526009 scopus 로고    scopus 로고
    • Deconvoluting the context-dependent role for autophagy in cancer
    • doi:10.1038/nrc3262
    • White, E. (2012). Deconvoluting the context-dependent role for autophagy in cancer. Nat. Rev. Cancer 12, 401-410. doi:10.1038/nrc3262.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 401-410
    • White, E.1
  • 135
    • 77951220669 scopus 로고    scopus 로고
    • Role of autophagy in suppression of inflammation and cancer
    • doi:10.1016/j.ceb.2009.12.008
    • White, E., Karp, C., Strohecker, A. M., Guo, Y., and Mathew, R. (2010). Role of autophagy in suppression of inflammation and cancer. Curr. Opin. Cell Biol. 22, 212-217. doi:10.1016/j.ceb.2009.12.008.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 212-217
    • White, E.1    Karp, C.2    Strohecker, A.M.3    Guo, Y.4    Mathew, R.5
  • 136
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • doi:10.1038/nchembio.79
    • Williams, A., Sarkar, S., Cuddon, P., Ttofi, E. K., Saiki, S., Siddiqi, F. H., et al. (2008). Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat. Chem. Biol. 4, 295-305. doi:10.1038/nchembio.79.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3    Ttofi, E.K.4    Saiki, S.5    Siddiqi, F.H.6
  • 137
    • 84866163103 scopus 로고    scopus 로고
    • Drosophila TRPML is required for TORC1 activation
    • doi:10.1016/j.cub.2012.06.055
    • Wong, C. O., Li, R., Montell, C., and Venkatachalam, K. (2012a). Drosophila TRPML is required for TORC1 activation. Curr. Biol. 22, 1616-1621. doi:10.1016/j.cub.2012.06.055.
    • (2012) Curr. Biol. , vol.22 , pp. 1616-1621
    • Wong, C.O.1    Li, R.2    Montell, C.3    Venkatachalam, K.4
  • 138
    • 82355170972 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore and calcium handling
    • doi:10.1007/978-1-61779-382-0_15
    • Wong, R., Steenbergen, C., and Murphy, E. (2012b). Mitochondrial permeability transition pore and calcium handling. Methods Mol. Biol. 810, 235-242. doi:10.1007/978-1-61779-382-0_15.
    • (2012) Methods Mol. Biol. , vol.810 , pp. 235-242
    • Wong, R.1    Steenbergen, C.2    Murphy, E.3
  • 139
    • 79952229430 scopus 로고    scopus 로고
    • Pancreatic cancers require autophagy for tumor growth
    • doi:10.1101/gad.2016111
    • Yang, S., Wang, X., Contino, G., Liesa, M., Sahin, E., Ying, H., et al. (2011a). Pancreatic cancers require autophagy for tumor growth. Genes Dev. 25, 717-729. doi:10.1101/gad.2016111.
    • (2011) Genes Dev. , vol.25 , pp. 717-729
    • Yang, S.1    Wang, X.2    Contino, G.3    Liesa, M.4    Sahin, E.5    Ying, H.6
  • 140
    • 80052697287 scopus 로고    scopus 로고
    • The role of autophagy in cancer:therapeutic implications
    • doi:10.1158/1535-7163.MCT-11-0047
    • Yang, Z. J., Chee, C. E., Huang, S., and Sinicrope, F. A. (2011b). The role of autophagy in cancer:therapeutic implications. Mol. Cancer Ther. 10, 1533-1541. doi:10.1158/1535-7163.MCT-11-0047.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 141
    • 33749162486 scopus 로고    scopus 로고
    • Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
    • doi:10.1038/ncb1482
    • Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T., Scapozza, L., et al. (2006). Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis. Nat. Cell Biol. 8, 1124-1132. doi:10.1038/ncb1482.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1124-1132
    • Yousefi, S.1    Perozzo, R.2    Schmid, I.3    Ziemiecki, A.4    Schaffner, T.5    Scapozza, L.6
  • 142
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • doi:10.1073/pnas.2436255100
    • Yue, Z., Jin, S., Yang, C., Levine, A. J., and Heintz, N. (2003). Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl. Acad. Sci. U.S.A. 100, 15077-15082. doi:10.1073/pnas.2436255100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 143
    • 67650270918 scopus 로고    scopus 로고
    • Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL
    • doi:10.4161/auto.5.5.8625
    • Zalckvar, E., Berissi, H., Eisenstein, M., and Kimchi, A. (2009a). Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL. Autophagy 5, 720-722. doi:10.4161/auto.5.5.8625.
    • (2009) Autophagy , vol.5 , pp. 720-722
    • Zalckvar, E.1    Berissi, H.2    Eisenstein, M.3    Kimchi, A.4
  • 144
    • 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
    • doi:10.1038/embor.2008.246
    • Zalckvar, E., Berissi, H., Mizrachy, L., Idelchuk, Y., Koren, I., Eisenstein, M., et al. (2009b). 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. 10, 285-292. doi:10.1038/embor.2008.246.
    • (2009) EMBO Rep. , vol.10 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3    Idelchuk, Y.4    Koren, I.5    Eisenstein, M.6
  • 145
    • 70349115675 scopus 로고    scopus 로고
    • A potentially dynamic lysosomal role for the endogenous TRPML proteins
    • doi:10.1002/path.2587
    • Zeevi, D. A., Frumkin, A., Offen-Glasner, V., Kogot-Levin, A., and Bach, G. (2009). A potentially dynamic lysosomal role for the endogenous TRPML proteins. J. Pathol. 219, 153-162. doi:10.1002/path.2587.
    • (2009) J. Pathol. , vol.219 , pp. 153-162
    • Zeevi, D.A.1    Frumkin, A.2    Offen-Glasner, V.3    Kogot-Levin, A.4    Bach, G.5
  • 146
    • 77956911289 scopus 로고    scopus 로고
    • Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy
    • doi:10.1242/jcs.067330
    • Zeevi, D. A., Lev, S., Frumkin, A., Minke, B., and Bach, G. (2010). Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy. J. Cell Sci. 123, 3112-3124. doi:10.1242/jcs.067330.
    • (2010) J. Cell Sci. , vol.123 , pp. 3112-3124
    • Zeevi, D.A.1    Lev, S.2    Frumkin, A.3    Minke, B.4    Bach, G.5
  • 147
    • 8544233547 scopus 로고    scopus 로고
    • Evidence that TRPM8 is an androgen-dependent Ca2+ channel required for the survival of prostate cancer cells
    • doi:10.1158/0008-5472.CAN-04-2146
    • Zhang, L., and Barritt, G. J. (2004). Evidence that TRPM8 is an androgen-dependent Ca2+ channel required for the survival of prostate cancer cells. Cancer Res. 64, 8365-8373. doi:10.1158/0008-5472.CAN-04-2146.
    • (2004) Cancer Res. , vol.64 , pp. 8365-8373
    • Zhang, L.1    Barritt, G.J.2
  • 148
    • 84864866637 scopus 로고    scopus 로고
    • Direct inhibition of the cold-activated TRPM8 ion channel by Galphaq
    • doi:10.1038/ncb2529
    • Zhang, X., Mak, S., Li, L., Parra, A., Denlinger, B., Belmonte, C., et al. (2012). Direct inhibition of the cold-activated TRPM8 ion channel by Galphaq. Nat. Cell Biol. 14, 851-858. doi:10.1038/ncb2529.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 851-858
    • Zhang, X.1    Mak, S.2    Li, L.3    Parra, A.4    Denlinger, B.5    Belmonte, C.6


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