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Volumn 44, Issue 2, 2004, Pages 295-307

Structure acquisition of the T1 domain of Kv1.3 during biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; POTASSIUM CHANNEL KV1.3; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 5144234840     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2004.09.011     Document Type: Article
Times cited : (51)

References (41)
  • 1
    • 0037636310 scopus 로고    scopus 로고
    • On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes. Derived on 20 October 2002 at the 28th FEBS Meeting in Istanbul
    • Agmon I., Auerbach T., Baram D., Bartels H., Bashan A., Berisio R., Fucini P., Hansen H.A., Harms J., Kessler M., et al. On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes. Derived on 20 October 2002 at the 28th FEBS Meeting in Istanbul. Eur. J. Biochem. 270:2003;2543-2556
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2543-2556
    • Agmon, I.1    Auerbach, T.2    Baram, D.3    Bartels, H.4    Bashan, A.5    Berisio, R.6    Fucini, P.7    Hansen, H.A.8    Harms, J.9    Kessler, M.10
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 a resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science. 289:2000;905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 4
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann R., Spahn C.M., Eswar N., Helmers J., Penczek P.A., Sali A., Frank J., Blobel G. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell. 107:2001;361-372
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 6
    • 0028465092 scopus 로고
    • Counting polymers moving through a single ion channel
    • Bezrukov S.M., Vodyanoy I., Parsegian V.A. Counting polymers moving through a single ion channel. Nature. 370:1994;279-281
    • (1994) Nature , vol.370 , pp. 279-281
    • Bezrukov, S.M.1    Vodyanoy, I.2    Parsegian, V.A.3
  • 7
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nanoscale pore
    • Bezrukov S.M., Vodyanoy I., Brutyan R.A., Kasianowicz J.J. Dynamics and free energy of polymers partitioning into a nanoscale pore. Macromolecules. 29:1996;8517-8522
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Brutyan, R.A.3    Kasianowicz, J.J.4
  • 10
    • 0009576440 scopus 로고
    • Conformational properties of polypeptide chains
    • (New York: W.H. Freeman and Company)
    • Creighton, T.E. (1993). Conformational properties of polypeptide chains. In Proteins (New York: W.H. Freeman and Company), pp. 171-199.
    • (1993) Proteins , pp. 171-199
    • Creighton, T.E.1
  • 14
    • 0042266913 scopus 로고    scopus 로고
    • A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels
    • Gu C., Jan Y.N., Jan L.Y. A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels. Science. 301:2003;646-649
    • (2003) Science , vol.301 , pp. 646-649
    • Gu, C.1    Jan, Y.N.2    Jan, L.Y.3
  • 15
    • 0034617121 scopus 로고    scopus 로고
    • Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels
    • Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science. 289:2000;123-127
    • (2000) Science , vol.289 , pp. 123-127
    • Gulbis, J.M.1    Zhou, M.2    Mann, S.3    MacKinnon, R.4
  • 18
    • 0037423401 scopus 로고    scopus 로고
    • Folding of the voltage-gated K+ channel T1 recognition domain
    • Kosolapov A., Deutsch C. Folding of the voltage-gated K+ channel T1 recognition domain. J. Biol. Chem. 278:2003;4305-4313
    • (2003) J. Biol. Chem. , vol.278 , pp. 4305-4313
    • Kosolapov, A.1    Deutsch, C.2
  • 19
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • Kowarik M., Kung S., Martoglio B., Helenius A. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell. 10:2002;769-778
    • (2002) Mol. Cell , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 21
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the Shaker potassium channel
    • Kreusch A., Pfaffinger P.J., Stevens C.F., Choe S. Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature. 392:1998;945-948
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 22
  • 24
    • 0026794064 scopus 로고
    • Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel
    • Li M., Jan Y., Jan L.Y. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science. 257:1992;1225-1230
    • (1992) Science , vol.257 , pp. 1225-1230
    • Li, M.1    Jan, Y.2    Jan, L.Y.3
  • 25
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao S., Lin J., Do H., Johnson A.E. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell. 90:1997;31-41
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 26
    • 0035818431 scopus 로고    scopus 로고
    • Pegylation: A method for assessing topological accessibilities in Kv1.3
    • Lu J., Deutsch C. Pegylation. a method for assessing topological accessibilities in Kv1.3 Biochemistry. 40:2001;13288-13301
    • (2001) Biochemistry , vol.40 , pp. 13288-13301
    • Lu, J.1    Deutsch, C.2
  • 27
    • 0035909067 scopus 로고    scopus 로고
    • T1-T1 interactions occur in ER membranes while nascent Kv peptides are still attached to ribosomes
    • Lu J., Robinson J.M., Edwards D., Deutsch C. T1-T1 interactions occur in ER membranes while nascent Kv peptides are still attached to ribosomes. Biochemistry. 40:2001;10934-10946
    • (2001) Biochemistry , vol.40 , pp. 10934-10946
    • Lu, J.1    Robinson, J.M.2    Edwards, D.3    Deutsch, C.4
  • 28
    • 0028955427 scopus 로고
    • The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane
    • Matlack K.E., Walter P. The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane. J. Biol. Chem. 270:1995;6170-6180
    • (1995) J. Biol. Chem. , vol.270 , pp. 6170-6180
    • Matlack, K.E.1    Walter, P.2
  • 30
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • Mingarro I., Nilsson I., Whitley P., von Heijne G. Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol. 1:2000;3
    • (2000) BMC Cell Biol. , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    Von Heijne, G.4
  • 31
    • 0034268781 scopus 로고    scopus 로고
    • The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel
    • Minor D.L., Lin Y.F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., Berger J.M. The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel. Cell. 102:2000;657-670
    • (2000) Cell , vol.102 , pp. 657-670
    • Minor, D.L.1    Lin, Y.F.2    Mobley, B.C.3    Avelar, A.4    Jan, Y.N.5    Jan, L.Y.6    Berger, J.M.7
  • 32
    • 0035025417 scopus 로고    scopus 로고
    • Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules
    • Movileanu L., Cheley S., Howorka S., Braha O., Bayley H. Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules. J. Gen. Physiol. 117:2001;239-251
    • (2001) J. Gen. Physiol. , vol.117 , pp. 239-251
    • Movileanu, L.1    Cheley, S.2    Howorka, S.3    Braha, O.4    Bayley, H.5
  • 33
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. The structural basis of ribosome activity in peptide bond synthesis. Science. 289:2000;920-930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 34
    • 0028244525 scopus 로고
    • Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit
    • Rettig J., Heinemann S.H., Wunder F., Lorra C., Parcej D.N., Dolly J.O., Pongs O. Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit. Nature. 369:1994;289-294
    • (1994) Nature , vol.369 , pp. 289-294
    • Rettig, J.1    Heinemann, S.H.2    Wunder, F.3    Lorra, C.4    Parcej, D.N.5    Dolly, J.O.6    Pongs, O.7
  • 36
    • 0029862913 scopus 로고    scopus 로고
    • Beta subunits promote K+ channel surface expression through effects early in biosynthesis
    • Shi G., Nakahira K., Hammond S., Rhodes K.J., Schechter L.E., Trimmer J.S. Beta subunits promote K+ channel surface expression through effects early in biosynthesis. Neuron. 16:1996;843-852
    • (1996) Neuron , vol.16 , pp. 843-852
    • Shi, G.1    Nakahira, K.2    Hammond, S.3    Rhodes, K.J.4    Schechter, L.E.5    Trimmer, J.S.6
  • 37
    • 0032525163 scopus 로고    scopus 로고
    • Different conformations of nascent peptides on ribosomes
    • Tsalkova T., Odom O.W., Kramer G., Hardesty B. Different conformations of nascent peptides on ribosomes. J. Mol. Biol. 278:1998;713-723
    • (1998) J. Mol. Biol. , vol.278 , pp. 713-723
    • Tsalkova, T.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4
  • 39
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead C.A., McCormick P.J., Johnson A.E. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell. 116:2004;725-736
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 40
    • 0028844541 scopus 로고
    • Assembly of voltage-gated potassium channels. Conserved hydrophilic motifs determine subfamily-specific interactions between the α-subunits
    • Xu J., Yu W., Jan J.N., Jan L., Li M. Assembly of voltage-gated potassium channels. Conserved hydrophilic motifs determine subfamily-specific interactions between the α-subunits. J. Biol. Chem. 270:1995;24761-24768
    • (1995) J. Biol. Chem. , vol.270 , pp. 24761-24768
    • Xu, J.1    Yu, W.2    Jan, J.N.3    Jan, L.4    Li, M.5
  • 41
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang N., George A.L., Horn R. Molecular basis of charge movement in voltage-gated sodium channels. Neuron. 16:1996;113-122
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.1    George, A.L.2    Horn, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.