메뉴 건너뛰기




Volumn 13, Issue 4, 2011, Pages 453-462

Lysosomal positioning coordinates cellular nutrient responses

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1;

EID: 79953316595     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2204     Document Type: Article
Times cited : (680)

References (43)
  • 1
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • DOI 10.1083/jcb.108.3.855
    • Heuser, J. Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell Biol. 108, 855-864 (1989). (Pubitemid 19083739)
    • (1989) Journal of Cell Biology , vol.108 , Issue.3 , pp. 855-864
    • Heuser, J.1
  • 3
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak, Y. et al. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303 (2010).
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1
  • 5
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: From peripheral formation to kiss-and-run fusion with lysosomes
    • DOI 10.1111/j.1600-0854.2008.00701.x
    • Jahreiss, L., Menzies, F. M. & Rubinsztein, D. C. The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Trafic 9, 574-587 (2008). (Pubitemid 351351616)
    • (2008) Traffic , vol.9 , Issue.4 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 6
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophago-somes mediates eficient encounters with lysosomes
    • Kimura, S., Noda, T. & Yoshimori, T. Dynein-dependent movement of autophago-somes mediates eficient encounters with lysosomes. Cell Struct. Funct. 33, 109-122 (2008).
    • (2008) Cell Struct. Funct. , vol.33 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 7
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • DOI 10.1038/nrm2245, PII NRM2245
    • Klionsky, D. J. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931-937 (2007). (Pubitemid 47622558)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 931-937
    • Klionsky, D.J.1
  • 8
    • 69449093622 scopus 로고    scopus 로고
    • Mammalian macroautophagy at a glance
    • Ravikumar, B. et al. Mammalian macroautophagy at a glance. J. Cell Sci. 122, 1707-1711 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1707-1711
    • Ravikumar, B.1
  • 9
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta, S., Peterson, T. R. & Sabatini, D. M. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol. Cell 40, 310-322 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 10
    • 0141733228 scopus 로고    scopus 로고
    • Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase/Akt-dependent and -independent phosphorylation of tuberin
    • DOI 10.1074/jbc.M303257200
    • Tee, A. R., Anjum, R. & Blenis, J. Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase/Akt-dependent and -independent phosphorylation of tuberin. J. Biol. Chem. 278, 37288-37296 (2003). (Pubitemid 37175245)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37288-37296
    • Tee, A.R.1    Anjum, R.2    Blenis, J.3
  • 11
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous Sclerosis Complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • DOI 10.1016/S0960-9822(03)00506-2
    • Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C. & Blenis, J. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13, 1259-1268 (2003). (Pubitemid 36953298)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 12
    • 34147133469 scopus 로고    scopus 로고
    • SnapShot: MTOR signaling
    • Soulard, A. & Hall, M. N. SnapShot: mTOR signaling. Cell 129, 434 (2007).
    • (2007) Cell , vol.129 , pp. 434
    • Soulard, A.1    Hall, M.N.2
  • 14
    • 33646111903 scopus 로고    scopus 로고
    • Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning
    • Cai, S. L. et al. Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning. J. Cell Biol. 173, 279-289 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 279-289
    • Cai, S.L.1
  • 15
    • 52949126962 scopus 로고    scopus 로고
    • Constitutively active Rheb induces oncogenic transformation
    • Jiang, H. & Vogt, P. K. Constitutively active Rheb induces oncogenic transformation. Oncogene 27, 5729-5740 (2008).
    • (2008) Oncogene , vol.27 , pp. 5729-5740
    • Jiang, H.1    Vogt, P.K.2
  • 16
    • 0032531562 scopus 로고    scopus 로고
    • KIF2β, a new kinesin superfamily protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation
    • DOI 10.1093/emboj/17.20.5855
    • Santama, N. et al. KIF2, a new kinesin superfamily protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation. EMBO J. 17, 5855-5867 (1998). (Pubitemid 28474780)
    • (1998) EMBO Journal , vol.17 , Issue.20 , pp. 5855-5867
    • Santama, N.1    Krijnse-Locker, J.2    Griffiths, G.3    Noda, Y.4    Hirokawa, N.5    Dotti, C.G.6
  • 17
    • 1642327748 scopus 로고    scopus 로고
    • A novel kinesin-like protein, KIF1Bβ3 is involved in the movement of lysosomes ot the cell periphery in non-neuronal cells
    • DOI 10.1111/j.1600-0854.2003.00165.x
    • Matsushita, M., Tanaka, S., Nakamura, N., Inoue, H. & Kanazawa, H. A novel kinesin-like protein, KIF1Bβ3 is involved in the movement of lysosomes to the cell periphery in non-neuronal cells. Trafic 5, 140-151 (2004). (Pubitemid 38379934)
    • (2004) Traffic , vol.5 , Issue.3 , pp. 140-151
    • Matsushita, M.1    Tanaka, S.2    Nakamura, N.3    Inoue, H.4    Kanazawa, H.5
  • 18
    • 33646192021 scopus 로고    scopus 로고
    • The Arf-family protein, Arl8b, is involved in the spatial distribution of lysosomes
    • Bagshaw, R. D., Callahan, J. W. & Mahuran, D. J. The Arf-family protein, Arl8b, is involved in the spatial distribution of lysosomes. Biochem. Biophys. Res. Commun. 344, 1186-1191 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 1186-1191
    • Bagshaw, R.D.1    Callahan, J.W.2    Mahuran, D.J.3
  • 19
    • 33646174748 scopus 로고    scopus 로고
    • An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility
    • DOI 10.1242/jcs.02958
    • Hofmann, I. & Munro, S. An N-terminally acetylated Arf-like GTPase is localised to lysosomes and affects their motility. J. Cell Sci. 119, 1494-1503 (2006). (Pubitemid 43732978)
    • (2006) Journal of Cell Science , vol.119 , Issue.8 , pp. 1494-1503
    • Hofmann, I.1    Munro, S.2
  • 20
    • 7244231299 scopus 로고    scopus 로고
    • Novel small GTPase subfamily capable of associating with tubulin is required for chromosome segregation
    • DOI 10.1242/jcs.01347
    • Okai, T. et al. Novel small GTPase subfamily capable of associating with tubulin is required for chromosome segregation. J. Cell Sci. 117, 4705-4715 (2004). (Pubitemid 39433437)
    • (2004) Journal of Cell Science , vol.117 , Issue.20 , pp. 4705-4715
    • Okai, T.1    Araki, Y.2    Tada, M.3    Tateno, T.4    Kontani, K.5    Katada, T.6
  • 21
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • Kimura, S., Noda, T. & Yoshimori, T. Dissection of the autophagosome maturation process by a novel reporter protein, tandem-uorescent-tagged LC3. Autophagy 3, 452-460 (2007). (Pubitemid 47293726)
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 22
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida, I., Minematsu-Ikeguchi, N., Ueno, T. & Kominami, E. Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 1, 84-91 (2005).
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 23
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R. & Rubinsztein, D. C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11, 1107-1117 (2002). (Pubitemid 34521091)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 25
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • DOI 10.1016/j.cell.2004.11.038, PII S0092867404011067
    • Gutierrez, M. G. et al. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753-766 (2004). (Pubitemid 40017683)
    • (2004) Cell , vol.119 , Issue.6 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 26
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • DOI 10.1126/science.1129577
    • Singh, S. B., Davis, A. S., Taylor, G. A. & Deretic, V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 313, 1438-1441 (2006). (Pubitemid 44360272)
    • (2006) Science , vol.313 , Issue.5792 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 27
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • DOI 10.1242/jcs.00703
    • Merlot, S. & Firtel, R. A. Leading the way: directional sensing through phosphatidylinositol 3-kinase and other signaling pathways. J. Cell Sci. 116, 3471-3478 (2003). (Pubitemid 37063391)
    • (2003) Journal of Cell Science , vol.116 , Issue.17 , pp. 3471-3478
    • Merlot, S.1    Firtel, R.A.2
  • 28
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • DOI 10.1038/nrc1949, PII NRC1949
    • Mohamed, M. M. & Sloane, B. F. Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6, 764-775 (2006). (Pubitemid 44450465)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.10 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 30
    • 0028948491 scopus 로고
    • KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B
    • Noda, Y., Sato-Yoshitake, R., Kondo, S., Nangaku, M. & Hirokawa, N. KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B. J. Cell Biol. 129, 157-167 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 157-167
    • Noda, Y.1    Sato-Yoshitake, R.2    Kondo, S.3    Nangaku, M.4    Hirokawa, N.5
  • 33
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar, S. et al. A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17, 170-178 (2008).
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1
  • 35
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov, D. D. et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14, 1296-1302 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1
  • 36
    • 33748572921 scopus 로고    scopus 로고
    • Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic
    • DOI 10.1111/j.1600-0854.2006.00475.x
    • Pryor, P. R., Reimann, F., Gribble, F. M. & Luzio, J. P. Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide trafic. Trafic 7, 1388-1398 (2006). (Pubitemid 44364176)
    • (2006) Traffic , vol.7 , Issue.10 , pp. 1388-1398
    • Pryor, P.R.1    Reimann, F.2    Gribble, F.M.3    Luzio, J.P.4
  • 37
    • 67049158203 scopus 로고    scopus 로고
    • Rheb controls misfolded protein metabolism by inhibiting aggresome formation and autophagy
    • Zhou, X. et al. Rheb controls misfolded protein metabolism by inhibiting aggresome formation and autophagy. Proc. Natl Acad. Sci. USA 106, 8923-8928 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8923-8928
    • Zhou, X.1
  • 38
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk, V. I., Mansilla, A., Menzies, F. M. & Rubinsztein, D. C. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol. Cell 33, 517-527 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 39
    • 0037147147 scopus 로고    scopus 로고
    • Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-α
    • DOI 10.1074/jbc.M208915200
    • Tafani, M. et al. Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-fi. J. Biol. Chem. 277, 49569-49576 (2002). (Pubitemid 36014396)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49569-49576
    • Tafani, M.1    Cohn, J.A.2    Karpinich, N.O.3    Rothman, R.J.4    Russo, M.A.5    Farber, J.L.6
  • 41
    • 65249089754 scopus 로고    scopus 로고
    • Methodological considerations for assessing autophagy modulators: A study with calcium phosphate precipitates
    • Sarkar, S., Korolchuk, V., Renna, M., Winslow, A. & Rubinsztein, D. C. Methodological considerations for assessing autophagy modulators: a study with calcium phosphate precipitates. Autophagy 5, 307-313 (2009).
    • (2009) Autophagy , vol.5 , pp. 307-313
    • Sarkar, S.1    Korolchuk, V.2    Renna, M.3    Winslow, A.4    Rubinsztein, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.