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Volumn 18, Issue 2, 2010, Pages 324-331

Rapid Inactivation of Proteins by Rapamycin-Induced Rerouting to Mitochondria

Author keywords

CELLBIO; PROTEINS

Indexed keywords

ADAPTOR PROTEIN; DEOXYRIBONUCLEASE II; FK 506 BINDING PROTEIN; RAPAMYCIN; SMALL INTERFERING RNA; SOMATOMEDIN B RECEPTOR; TRANSFERRIN;

EID: 76249107656     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2009.12.015     Document Type: Article
Times cited : (189)

References (39)
  • 1
    • 0028984226 scopus 로고
    • Expression and localisation of α-adaptin isoforms
    • Ball C.L., Hunt S.P., and Robinson M.S. Expression and localisation of α-adaptin isoforms. J. Cell Sci. 108 (1995) 2865-2875
    • (1995) J. Cell Sci. , vol.108 , pp. 2865-2875
    • Ball, C.L.1    Hunt, S.P.2    Robinson, M.S.3
  • 2
    • 33748195107 scopus 로고    scopus 로고
    • A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules
    • Banaszynski L.A., Chen L.C., Maynard-Smith L.A., Ooi A.G., and Wandless T.J. A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126 (2006) 995-1004
    • (2006) Cell , vol.126 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.C.2    Maynard-Smith, L.A.3    Ooi, A.G.4    Wandless, T.J.5
  • 4
    • 30744467675 scopus 로고    scopus 로고
    • Rapamycin analogs with differential binding specificity permit orthogonal control of protein activity
    • Bayle J.H., Grimley J.S., Stankunas K., Gestwicki J.E., Wandless T.J., and Crabtree G.R. Rapamycin analogs with differential binding specificity permit orthogonal control of protein activity. Chem. Biol. 13 (2006) 99-107
    • (2006) Chem. Biol. , vol.13 , pp. 99-107
    • Bayle, J.H.1    Grimley, J.S.2    Stankunas, K.3    Gestwicki, J.E.4    Wandless, T.J.5    Crabtree, G.R.6
  • 6
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • Belshaw P.J., Ho S.N., Crabtree G.R., and Schreiber S.L. Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins. Proc. Natl. Acad. Sci. USA 93 (1996) 4604-4607
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 7
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino J.S., and Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7 (2006) 568-579
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 9
    • 37549057671 scopus 로고    scopus 로고
    • AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes
    • Canuel M., Lefrancois S., Zeng J., and Morales C.R. AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes. Biochem. Biophys. Res. Commun. 366 (2008) 724-730
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 724-730
    • Canuel, M.1    Lefrancois, S.2    Zeng, J.3    Morales, C.R.4
  • 10
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke H., Baba T., van der Bliek A.M., and Schmid S.L. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131 (1995) 69-80
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    van der Bliek, A.M.3    Schmid, S.L.4
  • 11
  • 12
    • 34250825312 scopus 로고    scopus 로고
    • Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation
    • Dwivedy A., Gertler F.B., Miller J., Holt C.E., and Lebrand C. Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation. Development 134 (2007) 2137-2146
    • (2007) Development , vol.134 , pp. 2137-2146
    • Dwivedy, A.1    Gertler, F.B.2    Miller, J.3    Holt, C.E.4    Lebrand, C.5
  • 13
    • 33646787753 scopus 로고    scopus 로고
    • The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast
    • Foote C., and Nothwehr S.F. The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast. J. Cell Biol. 173 (2006) 615-626
    • (2006) J. Cell Biol. , vol.173 , pp. 615-626
    • Foote, C.1    Nothwehr, S.F.2
  • 15
    • 0030863780 scopus 로고    scopus 로고
    • Proximity and orientation underlie signaling by the non-receptor tyrosine kinase ZAP70
    • Graef I.A., Holsinger L.J., Diver S., Schreiber S.L., and Crabtree G.R. Proximity and orientation underlie signaling by the non-receptor tyrosine kinase ZAP70. EMBO J. 16 (1997) 5618-5628
    • (1997) EMBO J. , vol.16 , pp. 5618-5628
    • Graef, I.A.1    Holsinger, L.J.2    Diver, S.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 16
    • 52049084405 scopus 로고    scopus 로고
    • The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes
    • Haruki H., Nishikawa J., and Laemmli U.K. The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Mol. Cell 31 (2008) 925-932
    • (2008) Mol. Cell , vol.31 , pp. 925-932
    • Haruki, H.1    Nishikawa, J.2    Laemmli, U.K.3
  • 20
    • 21444442055 scopus 로고    scopus 로고
    • An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways
    • Inoue T., Heo W.D., Grimley J.S., Wandless T.J., and Meyer T. An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways. Nat. Methods 2 (2005) 415-418
    • (2005) Nat. Methods , vol.2 , pp. 415-418
    • Inoue, T.1    Heo, W.D.2    Grimley, J.S.3    Wandless, T.J.4    Meyer, T.5
  • 21
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels M.M., and Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J. 21 (2002) 6083-6094
    • (2002) EMBO J. , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 22
    • 34548510349 scopus 로고    scopus 로고
    • HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2
    • Lubben N.B., Sahlender D.A., Motley A.M., Lehner P.J., Benaroch P., and Robinson M.S. HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2. Mol. Biol. Cell 18 (2007) 3351-3365
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3351-3365
    • Lubben, N.B.1    Sahlender, D.A.2    Motley, A.M.3    Lehner, P.J.4    Benaroch, P.5    Robinson, M.S.6
  • 24
    • 0034657033 scopus 로고    scopus 로고
    • mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phsophate receptors
    • Meyer C., Zizioli D., Lausmann S., Eskelinen E.L., Hamann J., Saftig P., von Figura K., and Schu P. mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phsophate receptors. EMBO J. 19 (2000) 2193-2203
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    von Figura, K.7    Schu, P.8
  • 25
    • 0345255765 scopus 로고    scopus 로고
    • Targeted chemical disruption of clathrin function in living cells
    • Moskowitz H.S., Heuser J., McGraw T.E., and Ryan T.A. Targeted chemical disruption of clathrin function in living cells. Mol. Biol. Cell 14 (2003) 4437-4447
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4437-4447
    • Moskowitz, H.S.1    Heuser, J.2    McGraw, T.E.3    Ryan, T.A.4
  • 29
    • 0742269687 scopus 로고    scopus 로고
    • Golgi membranes remain segregated from the endoplasmic reticulum during mitosis in mammalian cells
    • Pecot M.Y., and Malhotra V. Golgi membranes remain segregated from the endoplasmic reticulum during mitosis in mammalian cells. Cell 116 (2004) 99-107
    • (2004) Cell , vol.116 , pp. 99-107
    • Pecot, M.Y.1    Malhotra, V.2
  • 30
    • 0035966098 scopus 로고    scopus 로고
    • The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
    • Peden A.A., Park G.Y., and Scheller R.H. The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding. J. Biol. Chem. 276 (2001) 49183-49187
    • (2001) J. Biol. Chem. , vol.276 , pp. 49183-49187
    • Peden, A.A.1    Park, G.Y.2    Scheller, R.H.3
  • 32
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson M.S. Adaptable adaptors for coated vesicles. Trends Cell Biol. 14 (2004) 167-174
    • (2004) Trends Cell Biol. , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 33
    • 17844387148 scopus 로고    scopus 로고
    • The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins
    • Sleat D.E., Lackland H., Wang Y., Sohar I., Xiao G., Li H., and Lobel P. The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins. Proteomics 5 (2005) 1520-1522
    • (2005) Proteomics , vol.5 , pp. 1520-1522
    • Sleat, D.E.1    Lackland, H.2    Wang, Y.3    Sohar, I.4    Xiao, G.5    Li, H.6    Lobel, P.7
  • 36
    • 0027174945 scopus 로고
    • Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone
    • Takizawa P.A., Yucel J.K., Veit B., Faulkner D.J., Deerinck T., Soto G., Ellisman M., and Malhotra V. Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone. Cell 73 (1993) 1079-1090
    • (1993) Cell , vol.73 , pp. 1079-1090
    • Takizawa, P.A.1    Yucel, J.K.2    Veit, B.3    Faulkner, D.J.4    Deerinck, T.5    Soto, G.6    Ellisman, M.7    Malhotra, V.8
  • 39
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • Zoncu R., Perera R.M., Balkin D.M., Pirruccello M., Toomre D., and De Camilli P. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell 136 (2009) 1110-1121
    • (2009) Cell , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.