메뉴 건너뛰기




Volumn 111, Issue 14, 2014, Pages

Protein phosphatase PP1/GLC7 interaction domain in yeast eIF2γ bypasses targeting subunit requirement for eIF2α dephosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; INITIATION FACTOR 2; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 2GAMMA; PHOSPHOPROTEIN PHOSPHATASE 1; TRANSCRIPTION FACTOR GCN4; UNCLASSIFIED DRUG;

EID: 84898028296     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1400129111     Document Type: Article
Times cited : (22)

References (66)
  • 1
    • 0027973793 scopus 로고
    • Reconstitution of ATPdependent aminophospholipid translocation in proteoliposomes
    • Auland ME, Roufogalis BD, Devaux PF, Zachowski A (1994) Reconstitution of ATPdependent aminophospholipid translocation in proteoliposomes. Proc Natl Acad Sci USA 91(23):10938-10942.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.23 , pp. 10938-10942
    • Auland, M.E.1    Roufogalis, B.D.2    Devaux, P.F.3    Zachowski, A.4
  • 2
    • 70349731740 scopus 로고    scopus 로고
    • Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast
    • Zhou X, Graham TR (2009) Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast. Proc Natl Acad Sci USA 106(39):16586-16591.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.39 , pp. 16586-16591
    • Zhou, X.1    Graham, T.R.2
  • 3
    • 70450242726 scopus 로고    scopus 로고
    • Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes
    • Coleman JA, Kwok MCM, Molday RS (2009) Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes. J Biol Chem 284(47):32670-32679.
    • (2009) J Biol Chem , vol.284 , Issue.47 , pp. 32670-32679
    • Coleman, J.A.1    Kwok, M.C.M.2    Molday, R.S.3
  • 4
    • 67649279563 scopus 로고    scopus 로고
    • P4 ATPases-lipid flippases and their role in disease
    • Folmer DE, Elferink RP, Paulusma CC (2009) P4 ATPases-lipid flippases and their role in disease. Biochim Biophys Acta 1791(7):628-635.
    • (2009) Biochim Biophys Acta , vol.1791 , Issue.7 , pp. 628-635
    • Folmer, D.E.1    Elferink, R.P.2    Paulusma, C.C.3
  • 5
    • 67649867465 scopus 로고    scopus 로고
    • ATP8B1 is essential for maintaining normal hearing
    • Stapelbroek JM, et al. (2009) ATP8B1 is essential for maintaining normal hearing. Proc Natl Acad Sci USA 106(24):9709-9714.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.24 , pp. 9709-9714
    • Stapelbroek, J.M.1
  • 6
    • 84155163114 scopus 로고    scopus 로고
    • Atp8a1 deficiency is associated with phosphatidylserine externalization in hippocampus and delayed hippocampus-dependent learning
    • Levano K, et al. (2012) Atp8a1 deficiency is associated with phosphatidylserine externalization in hippocampus and delayed hippocampus-dependent learning. J Neurochem 120(2):302-313.
    • (2012) J Neurochem , vol.120 , Issue.2 , pp. 302-313
    • Levano, K.1
  • 7
    • 84873132350 scopus 로고    scopus 로고
    • Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport
    • Coleman JA, Quazi F, Molday RS (2013) Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport. Biochim Biophys Acta 1831(3):555-574.
    • (2013) Biochim Biophys Acta , vol.1831 , Issue.3 , pp. 555-574
    • Coleman, J.A.1    Quazi, F.2    Molday, R.S.3
  • 8
    • 67349157973 scopus 로고    scopus 로고
    • How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane
    • Toyoshima C (2009) How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane. Biochim Biophys Acta 1793(6):941-946.
    • (2009) Biochim Biophys Acta , vol.1793 , Issue.6 , pp. 941-946
    • Toyoshima, C.1
  • 9
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase: Design of a perfect chemi-osmotic pump
    • Møller JV, Olesen C, Winther A-ML, Nissen P (2010) The sarcoplasmic Ca2+-ATPase: Design of a perfect chemi-osmotic pump. Q Rev Biophys 43(4):501-566.
    • (2010) Q Rev Biophys , vol.43 , Issue.4 , pp. 501-566
    • Møller, J.V.1    Olesen, C.2    A-Ml, W.3    Nissen, P.4
  • 10
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post RL, Hegyvary C, Kume S (1972) Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J Biol Chem 247(20):6530-6540.
    • (1972) J Biol Chem , vol.247 , Issue.20 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 11
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers RW (1967) Biochemical aspects of active transport. Annu Rev Biochem 36: 727-756.
    • (1967) Annu Rev Biochem , vol.36 , pp. 727-756
    • Albers, R.W.1
  • 12
    • 84857136080 scopus 로고    scopus 로고
    • Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2
    • Coleman JA, Vestergaard AL, Molday RS, Vilsen B, Andersen JP (2012) Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2. Proc Natl Acad Sci USA 109(5):1449-1454.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.5 , pp. 1449-1454
    • Coleman, J.A.1    Vestergaard, A.L.2    Molday, R.S.3    Vilsen, B.4    Andersen, J.P.5
  • 13
    • 84857129152 scopus 로고    scopus 로고
    • Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
    • Baldridge RD, Graham TR (2012) Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases. Proc Natl Acad Sci USA 109(6): E290-E298.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.6
    • Baldridge, R.D.1    Graham, T.R.2
  • 14
    • 84863650062 scopus 로고    scopus 로고
    • Outside of the box: Recent news about phospholipid translocation by P4 ATPases
    • Stone A, Williamson P (2012) Outside of the box: Recent news about phospholipid translocation by P4 ATPases. J Chem Biol 5(4):131-136.
    • (2012) J Chem Biol , vol.5 , Issue.4 , pp. 131-136
    • Stone, A.1    Williamson, P.2
  • 15
    • 84873113579 scopus 로고    scopus 로고
    • Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases
    • Baldridge RD, Graham TR (2013) Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases. Proc Natl Acad Sci USA 110(5):E358-E367.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.5
    • Baldridge, R.D.1    Graham, T.R.2
  • 16
    • 84880047409 scopus 로고    scopus 로고
    • Type IV P-type ATPases distinguish monoversus diacyl phosphatidylserine using a cytofacial exit gate in the membrane domain
    • Baldridge RD, Xu P, Graham TR (2013) Type IV P-type ATPases distinguish monoversus diacyl phosphatidylserine using a cytofacial exit gate in the membrane domain. J Biol Chem 288(27):19516-19527.
    • (2013) J Biol Chem , vol.288 , Issue.27 , pp. 19516-19527
    • Baldridge, R.D.1    Xu, P.2    Graham, T.R.3
  • 17
    • 0032483082 scopus 로고    scopus 로고
    • Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms
    • Vilsen B, Andersen JP (1998) Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry 37(31): 10961-10971.
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 10961-10971
    • Vilsen, B.1    Andersen, J.P.2
  • 18
    • 37249043376 scopus 로고    scopus 로고
    • The structural basis of calcium transport by the calcium pump
    • Olesen C, et al. (2007) The structural basis of calcium transport by the calcium pump. Nature 450(7172):1036-1042.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1036-1042
    • Olesen, C.1
  • 19
    • 0024826344 scopus 로고
    • Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2+-ATPase of sarcoplasmic reticulum
    • Vilsen B, Andersen JP, Clarke DM, MacLennan DH (1989) Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2+-ATPase of sarcoplasmic reticulum. J Biol Chem 264(35):21024-21030.
    • (1989) J Biol Chem , vol.264 , Issue.35 , pp. 21024-21030
    • Vilsen, B.1    Andersen, J.P.2    Clarke, D.M.3    Maclennan, D.H.4
  • 20
    • 0026785292 scopus 로고
    • Functional consequences of alterations to Gly310, Gly770, and Gly801 located in the transmembrane domain of the Ca2+-ATPase of sarcoplasmic reticulum
    • Andersen JP, Vilsen B, MacLennan DH (1992) Functional consequences of alterations to Gly310, Gly770, and Gly801 located in the transmembrane domain of the Ca2+-ATPase of sarcoplasmic reticulum. J Biol Chem 267(4):2767-2774.
    • (1992) J Biol Chem , vol.267 , Issue.4 , pp. 2767-2774
    • Andersen, J.P.1    Vilsen, B.2    Maclennan, D.H.3
  • 21
    • 0030836853 scopus 로고    scopus 로고
    • Leucine 332 at the boundary between the fourth transmembrane segment and the cytoplasmic domain of Na+,K+-ATPase plays a pivotal role in the ion translocating conformational changes
    • Vilsen B (1997) Leucine 332 at the boundary between the fourth transmembrane segment and the cytoplasmic domain of Na+,K+-ATPase plays a pivotal role in the ion translocating conformational changes. Biochemistry 36(43):13312-13324.
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13312-13324
    • Vilsen, B.1
  • 22
    • 84874110716 scopus 로고    scopus 로고
    • Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion
    • Emre Onat O, et al. (2013) Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion. Eur J Hum Genet 21(3):281-285.
    • (2013) Eur J Hum Genet , vol.21 , Issue.3 , pp. 281-285
    • Emre Onat, O.1
  • 23
    • 79955763752 scopus 로고    scopus 로고
    • Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2
    • Coleman JA, Molday RS (2011) Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2. J Biol Chem 286(19):17205-17216.
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 17205-17216
    • Coleman, J.A.1    Molday, R.S.2
  • 25
    • 78650479478 scopus 로고    scopus 로고
    • A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps
    • Morth JP, et al. (2011) A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps. Nat Rev Mol Cell Biol 12(1):60-70.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.1 , pp. 60-70
    • Morth, J.P.1
  • 26
    • 79951746312 scopus 로고    scopus 로고
    • Phospholipid transport: Sighting a new face of an old friend
    • Williamson P (2011) Phospholipid transport: Sighting a new face of an old friend. Curr Biol 21(4):R168-R169.
    • (2011) Curr Biol , vol.21 , Issue.4
    • Williamson, P.1
  • 27
    • 78549241926 scopus 로고    scopus 로고
    • Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo balanced translocation and a severe neurological phenotype
    • Cacciagli P, et al. (2010) Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo balanced translocation and a severe neurological phenotype. Eur J Hum Genet 18(12):1360-1363.
    • (2010) Eur J Hum Genet , vol.18 , Issue.12 , pp. 1360-1363
    • Cacciagli, P.1
  • 28
    • 84866174651 scopus 로고    scopus 로고
    • Mutations in a P-type ATPase gene cause axonal degeneration
    • Zhu X, et al. (2012) Mutations in a P-type ATPase gene cause axonal degeneration. PLoS Genet 8(8):e1002853.
    • (2012) PLoS Genet , vol.8 , Issue.8
    • Zhu, X.1
  • 29
    • 79960033247 scopus 로고    scopus 로고
    • Crystal structure of a copper-transporting PIB-type ATPase
    • Gourdon P, et al. (2011) Crystal structure of a copper-transporting PIB-type ATPase. Nature 475(7354):59-64.
    • (2011) Nature , vol.475 , Issue.7354 , pp. 59-64
    • Gourdon, P.1
  • 30
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P1B-ATPases
    • Argüello JM, Eren E, González-GuerreroM (2007) The structure and function of heavy metal transport P1B-ATPases. Biometals 20(3-4):233-248.
    • (2007) Biometals , vol.20 , Issue.3-4 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    González-Guerrero, M.3
  • 32
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • Skou JC (1957) The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim Biophys Acta 23(2):394-401.
    • (1957) Biochim Biophys Acta , vol.23 , Issue.2 , pp. 394-401
    • Skou, J.C.1
  • 33
    • 67650527140 scopus 로고    scopus 로고
    • The C terminus of Na+,K+-ATPase controls Na+ affinity on both sides of the membrane through Arg935
    • Toustrup-Jensen MS, et al. (2009) The C terminus of Na+,K+-ATPase controls Na+ affinity on both sides of the membrane through Arg935. J Biol Chem 284(28): 18715-18725.
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 18715-18725
    • Toustrup-Jensen, M.S.1
  • 34
    • 0033620953 scopus 로고    scopus 로고
    • Mutant Phe788-> Leu of the Na+,K+-ATPase is inhibited by micromolar concentrations of potassium and exhibits high Na+-ATPase activity at low sodium concentrations
    • Vilsen B (1999) Mutant Phe788-> Leu of the Na+,K+-ATPase is inhibited by micromolar concentrations of potassium and exhibits high Na+-ATPase activity at low sodium concentrations. Biochemistry 38(35):11389-11400.
    • (1999) Biochemistry , vol.38 , Issue.35 , pp. 11389-11400
    • Vilsen, B.1
  • 35
    • 36549076985 scopus 로고    scopus 로고
    • On the origin of lipid asymmetry: The flip side of ion transport
    • Lenoir G, Williamson P, Holthuis JCM (2007) On the origin of lipid asymmetry: The flip side of ion transport. Curr Opin Chem Biol 11(6):654-661.
    • (2007) Curr Opin Chem Biol , vol.11 , Issue.6 , pp. 654-661
    • Lenoir, G.1    Williamson, P.2    Holthuis, J.C.M.3
  • 36
    • 77958066477 scopus 로고    scopus 로고
    • Defect-mediated trafficking across cell membranes: Insights from in silico modeling
    • Gurtovenko AA, Anwar J, Vattulainen I (2010) Defect-mediated trafficking across cell membranes: Insights from in silico modeling. Chem Rev 110(10):6077-6103.
    • (2010) Chem Rev , vol.110 , Issue.10 , pp. 6077-6103
    • Gurtovenko, A.A.1    Anwar, J.2    Vattulainen, I.3
  • 37
    • 84856000743 scopus 로고    scopus 로고
    • Tracing cytoplasmic Ca2+ ion and water access points in the Ca2+-ATPase
    • Musgaard M, Thøgersen L, Schiøtt B, Tajkhorshid E (2012) Tracing cytoplasmic Ca2+ ion and water access points in the Ca2+-ATPase. Biophys J 102(2):268-277.
    • (2012) Biophys J , vol.102 , Issue.2 , pp. 268-277
    • Musgaard, M.1    Thøgersen, L.2    Schiøtt, B.3    Tajkhorshid, E.4
  • 38
    • 38349129384 scopus 로고    scopus 로고
    • Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2+-ATPase, the gatekeeper and the pivot
    • Einholm AP, Andersen JP, Vilsen B (2007) Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2+-ATPase, the gatekeeper and the pivot. J Bioenerg Biomembr 39(5-6):357-366.
    • (2007) J Bioenerg Biomembr , vol.39 , Issue.5-6 , pp. 357-366
    • Einholm, A.P.1    Andersen, J.P.2    Vilsen, B.3
  • 39
    • 34548221029 scopus 로고    scopus 로고
    • Importance of Leu99 in transmembrane segment M1 of the Na+, K+-ATPase in the binding and occlusion of K+
    • Einholm AP, Andersen JP, Vilsen B (2007) Importance of Leu99 in transmembrane segment M1 of the Na+, K+-ATPase in the binding and occlusion of K+. J Biol Chem 282(33):23854-23866.
    • (2007) J Biol Chem , vol.282 , Issue.33 , pp. 23854-23866
    • Einholm, A.P.1    Andersen, J.P.2    Vilsen, B.3
  • 40
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Lightning-fast iterative protein sequence searching by HMM-HMM alignment
    • Remmert M, Biegert A, Hauser A, Söding J (2012) HHblits: Lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat Methods 9(2):173-175.
    • (2012) Nat Methods , vol.9 , Issue.2 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Söding, J.4
  • 41
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding J, Biegert A, Lupas AN (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33(Web Server issue): W244-W248.
    • (2005) Nucleic Acids Res , vol.33 , Issue.WEB SERVER ISSUE.
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 43
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips JC, et al. (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26(16):1781-1802.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1781-1802
    • Phillips, J.C.1
  • 44
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks BR, et al. (2009) CHARMM: The biomolecular simulation program. J Comput Chem 30(10):1545-1614.
    • (2009) J Comput Chem , vol.30 , Issue.10 , pp. 1545-1614
    • Brooks, B.R.1
  • 45
    • 48549102871 scopus 로고    scopus 로고
    • United-atom acyl chains for CHARMM phospholipids
    • Hénin J, Shinoda W, Klein ML (2008) United-atom acyl chains for CHARMM phospholipids. J Phys Chem B 112(23):7008-7015.
    • (2008) J Phys Chem B , vol.112 , Issue.23 , pp. 7008-7015
    • Hénin, J.1    Shinoda, W.2    Klein, M.L.3
  • 46
    • 0035898611 scopus 로고    scopus 로고
    • Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR
    • Ung TL, Cao C, Lu J, Ozato K, Dever TE (2001) Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. EMBO J 20(14):3728-3737.
    • (2001) EMBO J , vol.20 , Issue.14 , pp. 3728-3737
    • Ung, T.L.1    Cao, C.2    Lu, J.3    Ozato, K.4    Dever, T.E.5
  • 47
    • 0030756298 scopus 로고    scopus 로고
    • Functional analysis of the nuclear LIM domain interactor NLI
    • Jurata LW, Gill GN (1997) Functional analysis of the nuclear LIM domain interactor NLI. Mol Cell Biol 17(10):5688-5698.
    • (1997) Mol Cell Biol , vol.17 , Issue.10 , pp. 5688-5698
    • Jurata, L.W.1    Gill, G.N.2
  • 48
    • 0032548838 scopus 로고    scopus 로고
    • Interactions between LIM domains and the LIM domain-binding protein Ldb1
    • Breen JJ, Agulnick AD, Westphal H, Dawid IB (1998) Interactions between LIM domains and the LIM domain-binding protein Ldb1. J Biol Chem 273(8):4712-4717.
    • (1998) J Biol Chem , vol.273 , Issue.8 , pp. 4712-4717
    • Breen, J.J.1    Agulnick, A.D.2    Westphal, H.3    Dawid, I.B.4
  • 49
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2 α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek SA, Zhu S, Wek RC (1995) The histidyl-tRNA synthetase-related sequence in the eIF-2 α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol Cell Biol 15(8):4497-4506.
    • (1995) Mol Cell Biol , vol.15 , Issue.8 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 50
    • 0034028905 scopus 로고    scopus 로고
    • Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase
    • Yang R, Wek SA, Wek RC (2000) Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase. Mol Cell Biol 20(8):2706-2717.
    • (2000) Mol Cell Biol , vol.20 , Issue.8 , pp. 2706-2717
    • Yang, R.1    Wek, S.A.2    Wek, R.C.3
  • 51
    • 69949167078 scopus 로고    scopus 로고
    • Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p
    • Zaborske JM, et al. (2009) Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p. J Biol Chem 284(37):25254-25267.
    • (2009) J Biol Chem , vol.284 , Issue.37 , pp. 25254-25267
    • Zaborske, J.M.1
  • 52
    • 0037382865 scopus 로고    scopus 로고
    • Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2
    • Cherkasova VA, Hinnebusch AG (2003) Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2. Genes Dev 17(7):859-872.
    • (2003) Genes Dev , vol.17 , Issue.7 , pp. 859-872
    • Cherkasova, V.A.1    Hinnebusch, A.G.2
  • 53
    • 33744957161 scopus 로고    scopus 로고
    • Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B e
    • Alone PV, Dever TE (2006) Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B e. J Biol Chem 281(18):12636-12644.
    • (2006) J Biol Chem , vol.281 , Issue.18 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 54
    • 34247111608 scopus 로고    scopus 로고
    • EIF2α phosphorylation in cellular stress responses and disease
    • eds Mathews MB, Sonenberg N, Hershey JWB (Cold Spring Harb Lab Press, Cold Spring Harbor, NY)
    • Ron D, Harding HP (2007) eIF2α phosphorylation in cellular stress responses and disease. Translational Control in Biology and Medicine, eds Mathews MB, Sonenberg N, Hershey JWB (Cold Spring Harb Lab Press, Cold Spring Harbor, NY), pp 345-368.
    • (2007) Translational Control in Biology and Medicine , pp. 345-368
    • Ron, D.1    Harding, H.P.2
  • 55
    • 57349198343 scopus 로고    scopus 로고
    • Control of cellular GADD34 levels by the 26S proteasome
    • Brush MH, Shenolikar S (2008) Control of cellular GADD34 levels by the 26S proteasome. Mol Cell Biol 28(23):6989-7000.
    • (2008) Mol Cell Biol , vol.28 , Issue.23 , pp. 6989-7000
    • Brush, M.H.1    Shenolikar, S.2
  • 56
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2α phosphatase, CReP, promotes survival of stressed cells
    • Jousse C, et al. (2003) Inhibition of a constitutive translation initiation factor 2α phosphatase, CReP, promotes survival of stressed cells. J Cell Biol 163(4):767-775.
    • (2003) J Cell Biol , vol.163 , Issue.4 , pp. 767-775
    • Jousse, C.1
  • 57
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • Novoa I, Zeng H, Harding HP, Ron D (2001) Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J Cell Biol 153(5): 1011-1022.
    • (2001) J Cell Biol , vol.153 , Issue.5 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 58
    • 0034808081 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor
    • Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S (2001) Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor Mol Cell Biol 21(20):6841-6850
    • (2001) Mol Cell Biol , vol.21 , Issue.20 , pp. 6841-6850
    • Connor, J.H.1    Weiser, D.C.2    Li, S.3    Hallenbeck, J.M.4    Shenolikar, S.5
  • 59
    • 55849085351 scopus 로고    scopus 로고
    • Translation initiation factor 2γ mutant alters start codon selection independent of Met-tRNA binding
    • Alone PV, Cao C, Dever TE (2008) Translation initiation factor 2γ mutant alters start codon selection independent of Met-tRNA binding. Mol Cell Biol 28(22):6877-6888.
    • (2008) Mol Cell Biol , vol.28 , Issue.22 , pp. 6877-6888
    • Alone, P.V.1    Cao, C.2    Dever, T.E.3
  • 60
    • 0025330827 scopus 로고
    • Identification of positiveacting domains in GCN2 protein kinase required for translational activation of GCN4 expression
    • Wek RC, Ramirez M, Jackson BM, Hinnebusch AG (1990) Identification of positiveacting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol Cell Biol 10(6):2820-2831.
    • (1990) Mol Cell Biol , vol.10 , Issue.6 , pp. 2820-2831
    • Wek, R.C.1    Ramirez, M.2    Jackson, B.M.3    Hinnebusch, A.G.4
  • 61
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2α substrate recognition
    • Dey M, et al. (2005) Mechanistic link between PKR dimerization, autophosphorylation, and eIF2α substrate recognition. Cell 122(6):901-913.
    • (2005) Cell , vol.122 , Issue.6 , pp. 901-913
    • Dey, M.1
  • 62
    • 0027182508 scopus 로고
    • Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast
    • Mitchell DA, Marshall TK, Deschenes RJ (1993) Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast 9(7):715-722.
    • (1993) Yeast , vol.9 , Issue.7 , pp. 715-722
    • Mitchell, D.A.1    Marshall, T.K.2    Deschenes, R.J.3
  • 63
    • 80555131009 scopus 로고    scopus 로고
    • Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAi( Met) ternary complex binding to the 40S ribosome
    • Shin BS, et al. (2011) Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAi( Met) ternary complex binding to the 40S ribosome. Nat Struct Mol Biol 18(11):1227-1234.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.11 , pp. 1227-1234
    • Shin, B.S.1
  • 64
    • 77953414533 scopus 로고    scopus 로고
    • Snf1 promotes phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 by activating Gcn2 and inhibiting phosphatases Glc7 and Sit4
    • Cherkasova V, Qiu H, Hinnebusch AG (2010) Snf1 promotes phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 by activating Gcn2 and inhibiting phosphatases Glc7 and Sit4. Mol Cell Biol 30(12):2862-2873.
    • (2010) Mol Cell Biol , vol.30 , Issue.12 , pp. 2862-2873
    • Cherkasova, V.1    Qiu, H.2    Hinnebusch, A.G.3
  • 65
    • 0031899816 scopus 로고    scopus 로고
    • Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2
    • Romano PR, et al. (1998) Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2. Mol Cell Biol 18(4):2282-2297.
    • (1998) Mol Cell Biol , vol.18 , Issue.4 , pp. 2282-2297
    • Romano, P.R.1
  • 66
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
    • Krishnamoorthy T, Pavitt GD, Zhang F, Dever TE, Hinnebusch AG (2001) Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol Cell Biol 21(15):5018-5030.
    • (2001) Mol Cell Biol , vol.21 , Issue.15 , pp. 5018-5030
    • Krishnamoorthy, T.1    Pavitt, G.D.2    Zhang, F.3    Dever, T.E.4    Hinnebusch, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.