메뉴 건너뛰기




Volumn 174, Issue 3, 2000, Pages 181-190

Topogenic motifs in P-type ATPases

Author keywords

Membrane insertion; P type ATPases; Polytopic membrane proteins; Subunit oligomerization; Topogenic motifs

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ION;

EID: 0034177737     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002320001042     Document Type: Review
Times cited : (25)

References (40)
  • 2
    • 0028902644 scopus 로고
    • Topology of the Na,K-ATPase: Evidence for externalization of a labile transmembrane structure during heating
    • Arystarkhova, E., Gibbons, D.L., Sweadner, K.J. 1995. Topology of the Na,K-ATPase: Evidence for externalization of a labile transmembrane structure during heating. J. Biol. Chem. 270:8785-8796
    • (1995) J. Biol. Chem. , vol.270 , pp. 8785-8796
    • Arystarkhova, E.1    Gibbons, D.L.2    Sweadner, K.J.3
  • 3
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen, K.B., Palmgren, M.G. 1998. Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46:84-101
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 5
    • 0028361579 scopus 로고
    • +-ATPase using in vitro translation
    • +-ATPase using in vitro translation. J. Biol. Chem. 269:16909-16919
    • (1994) J. Biol. Chem. , vol.269 , pp. 16909-16919
    • Bamberg, K.1    Sachs, G.2
  • 8
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle, D., Weeks, D., Sachs, G. 1995. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J. Biol. Chem. 270:25678-25684
    • (1995) J. Biol. Chem. , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 9
    • 0040888007 scopus 로고    scopus 로고
    • β-subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase α-subunit
    • Beggah, A.T., Béguin, P., Bamberg, K., Sachs, G., Geering, K. 1999. β-subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase α-subunit. J. Biol. Chem. 274:8217-8223
    • (1999) J. Biol. Chem. , vol.274 , pp. 8217-8223
    • Beggah, A.T.1    Béguin, P.2    Bamberg, K.3    Sachs, G.4    Geering, K.5
  • 10
    • 0032544363 scopus 로고    scopus 로고
    • Membrane integration of Na,K-ATPase α-subunits and β-subunit assembly
    • Béguin, P., Hasler, U., Beggah, A., Horisberger, J.D., Geering, K. 1998. Membrane integration of Na,K-ATPase α-subunits and β-subunit assembly. J. Biol. Chem. 273:24921-24931
    • (1998) J. Biol. Chem. , vol.273 , pp. 24921-24931
    • Béguin, P.1    Hasler, U.2    Beggah, A.3    Horisberger, J.D.4    Geering, K.5
  • 11
    • 0032497570 scopus 로고    scopus 로고
    • Protein targeting: Getting into the groove
    • Bernstein, H.D. 1998. Protein targeting: Getting into the groove. Curr. Biol. 8:R715-R718
    • (1998) Curr. Biol. , vol.8
    • Bernstein, H.D.1
  • 12
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77:1496-1500
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 13
    • 0031853133 scopus 로고    scopus 로고
    • Unusual degradation of α-β-complexes in Xenopus oocytes by β-subunits of Xenopus gastric H-K-ATPase
    • Chen, P.X., Mathews, P.M., Good, P.J., Rossier, B.C., Geering, K. 1998. Unusual degradation of α-β-complexes in Xenopus oocytes by β-subunits of Xenopus gastric H-K-ATPase. Am. J. Physiol. 44:C139-C145
    • (1998) Am. J. Physiol. , vol.44
    • Chen, P.X.1    Mathews, P.M.2    Good, P.J.3    Rossier, B.C.4    Geering, K.5
  • 14
    • 0030977127 scopus 로고    scopus 로고
    • Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system
    • Colonna, T.E., Huynh, L., Fambrough, D.M. 1997. Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system. J. Biol. Chem. 272:12366-12372
    • (1997) J. Biol. Chem. , vol.272 , pp. 12366-12372
    • Colonna, T.E.1    Huynh, L.2    Fambrough, D.M.3
  • 15
    • 0013669067 scopus 로고    scopus 로고
    • G. von Heijne, editor. Springer-Verlag, Heidelberg, Germany
    • Deber, C.M., Goto, N.K. 1997. In: Membrane Protein Assembly. G. von Heijne, editor. pp. 25-34. Springer-Verlag, Heidelberg, Germany
    • (1997) Membrane Protein Assembly , pp. 25-34
    • Deber, C.M.1    Goto, N.K.2
  • 20
    • 0028982165 scopus 로고
    • Topology of the α-subunit of Na,K-ATPase based on proteolysis lability of the topological organisation
    • Goldshleger, R., Tal, D.M., Karlish, S.J.D. 1995. Topology of the α-subunit of Na,K-ATPase based on proteolysis lability of the topological organisation. Biochemistry 34:8668-8679
    • (1995) Biochemistry , vol.34 , pp. 8668-8679
    • Goldshleger, R.1    Tal, D.M.2    Karlish, S.J.D.3
  • 21
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., Rapoport, T.A., Lodish, H.F. 1989. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 86:5786-5790
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 22
    • 0032515054 scopus 로고    scopus 로고
    • Role of β-subunit domains in the assembly, stable expression, intracellular routing and functional properties of Na,K-ATPase
    • Hasler, U., Wang, X., Crambert, G., Béguin, P., Jaisser, F., Horisberger J-D., Geering, K. 1998. Role of β-subunit domains in the assembly, stable expression, intracellular routing and functional properties of Na,K-ATPase. J. Biol. Chem. 273:30826-30835
    • (1998) J. Biol. Chem. , vol.273 , pp. 30826-30835
    • Hasler, U.1    Wang, X.2    Crambert, G.3    Béguin, P.4    Jaisser, F.5    Horisberger, J.-D.6    Geering, K.7
  • 23
    • 0032904215 scopus 로고    scopus 로고
    • Regulation of protein biogenesis at the endoplasmic reticulum membrane
    • Hegde, R.S., Lingappa, V.R. 1999. Regulation of protein biogenesis at the endoplasmic reticulum membrane. Trends Cell Biol. 9:132-137
    • (1999) Trends Cell Biol. , vol.9 , pp. 132-137
    • Hegde, R.S.1    Lingappa, V.R.2
  • 24
    • 0013690250 scopus 로고    scopus 로고
    • The biosynthesis of membrane proteins at the endoplasmic reticulum
    • G. von Heijne, editor. Springer-Verlag, Heidelberg, Germany
    • High, S., Laird, V., Olivier, J.D. 1997. The biosynthesis of membrane proteins at the endoplasmic reticulum. In: Membrane Protein Assembly. G. von Heijne, editor. pp. 119-131. Springer-Verlag, Heidelberg, Germany
    • (1997) Membrane Protein Assembly , pp. 119-131
    • High, S.1    Laird, V.2    Olivier, J.D.3
  • 26
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R.R. 1997. ER quality control: The cytoplasmic connection. Cell 88:427-430
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 28
    • 0001786054 scopus 로고    scopus 로고
    • Transmembrane α-helix interactions in folding and oligomerization of integral membrane proteins
    • G. von Heijne, editor, Springer-Verlag, Heidelberg, Germany
    • Lemmon, M.A., MacKenzie, K.R., Arkin, I.T., Engelman, D.M. 1997. Transmembrane α-helix interactions in folding and oligomerization of integral membrane proteins. In: Membrane Protein Assembly. G. von Heijne, editor, pp. 3-20. Springer-Verlag, Heidelberg, Germany
    • (1997) Membrane Protein Assembly , pp. 3-20
    • Lemmon, M.A.1    MacKenzie, K.R.2    Arkin, I.T.3    Engelman, D.M.4
  • 32
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • Lutsenko, S., Kaplan, J.H. 1995. Organization of P-type ATPases: Significance of structural diversity. Biochemistry 34:15607-15613
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 34
    • 0032080152 scopus 로고    scopus 로고
    • Regions of association between the α and the β subunit of the gastric H,K-ATPase
    • Melle-Milovanovic, D., Milovanovic, M., Nagpal, S., Sachs, G., Shin, J.M. 1998. Regions of association between the α and the β subunit of the gastric H,K-ATPase. J. Biol. Chem. 273:11075-11081
    • (1998) J. Biol. Chem. , vol.273 , pp. 11075-11081
    • Melle-Milovanovic, D.1    Milovanovic, M.2    Nagpal, S.3    Sachs, G.4    Shin, J.M.5
  • 35
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Moller, J.V., Juul, B., Lemaire, M. 1996. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286:1-51
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Lemaire, M.3
  • 36
    • 0030971046 scopus 로고    scopus 로고
    • Involvement of the M7/M8 extracellular loop of the sodium pump α subunit in ion transport. Structural and functional homology to P-loops of ion channels
    • Schneider, H., Scheiner-Bobis, G. 1997. Involvement of the M7/M8 extracellular loop of the sodium pump α subunit in ion transport. Structural and functional homology to P-loops of ion channels. J. Biol. Chem. 272:16158-16165
    • (1997) J. Biol. Chem. , vol.272 , pp. 16158-16165
    • Schneider, H.1    Scheiner-Bobis, G.2
  • 38
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., von Heijne, G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Prot. Sci. 7:1029-1038
    • (1998) Prot. Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 39
    • 0028977979 scopus 로고
    • 2-terminal third (H1-H4) of Na,K-ATPase α subunit alternately initiate and halt membrane translocation of the newly synthesized polypeptide
    • 2-terminal third (H1-H4) of Na,K-ATPase α subunit alternately initiate and halt membrane translocation of the newly synthesized polypeptide. J. Biol. Chem. 270:11985-11991
    • (1995) J. Biol. Chem. , vol.270 , pp. 11985-11991
    • Xie, Y.H.1    Morimoto, T.2
  • 40
    • 0029116124 scopus 로고
    • Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences
    • Zhang, J.T., Ling, V. 1995. Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences. Biochemistry 34:9159-9165
    • (1995) Biochemistry , vol.34 , pp. 9159-9165
    • Zhang, J.T.1    Ling, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.