메뉴 건너뛰기




Volumn 23, Issue 7, 2014, Pages 981-992

Folding of aquaporin 1: Multiple evidence that helix 3 can shift out of the membrane core

Author keywords

Hydrophobicity; Membrane protein; Molecular dynamics; Protein folding; Translocon recognition

Indexed keywords

AQUAPORIN 1; DNA; GLYCOSYLATED PROTEIN; MEMBRANE PROTEIN; AQUAPORIN 4;

EID: 84904179187     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2483     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J, Engelman D (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.1    Engelman, D.2
  • 2
    • 0034697967 scopus 로고    scopus 로고
    • The sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich S, Mothes W, Brunner J, Rapoport T (2000) The sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102:233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.1    Mothes, W.2    Brunner, J.3    Rapoport, T.4
  • 6
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G (1989) Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 8
    • 84865293045 scopus 로고    scopus 로고
    • A successful change of circumstance: A transition state for membrane protein folding
    • Booth P (2012) A successful change of circumstance: A transition state for membrane protein folding. Curr Opin Struct Biol 22:469-475.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 469-475
    • Booth, P.1
  • 9
    • 77954070546 scopus 로고    scopus 로고
    • Control of membrane protein topology by a single c-terminal residue
    • Seppala S, Slusky J, Lloris-Garcera P, Rapp M, von Heijne G (2010) Control of membrane protein topology by a single c-terminal residue. Science 328:1698-1700.
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppala, S.1    Slusky, J.2    Lloris-Garcera, P.3    Rapp, M.4    Von Heijne, G.5
  • 10
    • 51649107357 scopus 로고    scopus 로고
    • To flip or not to flip: Lipid-protein charge interactions are a determinant of final membrane protein topology
    • Bogdanov M, Xie J, Heacock P, Dowhan W (2008) To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology. J Cell Biol 182:925-935.
    • (2008) J Cell Biol , vol.182 , pp. 925-935
    • Bogdanov, M.1    Xie, J.2    Heacock, P.3    Dowhan, W.4
  • 11
    • 0031983038 scopus 로고    scopus 로고
    • Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator n terminus transmembrane assembly
    • Lu Y, Xiong X, Helm A, Kimani K, Bragin A, Skach W (1998) Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator n terminus transmembrane assembly. J Biol Chem 273:568-576.
    • (1998) J Biol Chem , vol.273 , pp. 568-576
    • Lu, Y.1    Xiong, X.2    Helm, A.3    Kimani, K.4    Bragin, A.5    Skach, W.6
  • 12
    • 66849131417 scopus 로고    scopus 로고
    • Cellular mechanisms of membrane protein folding
    • Skach W (2009) Cellular mechanisms of membrane protein folding. Nat Struct Mol Biol 16:606-612.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 606-612
    • Skach, W.1
  • 14
    • 70350040736 scopus 로고    scopus 로고
    • Cell penetrating peptides: How do they do it?
    • Herce H, Garcia A (2007) Cell penetrating peptides: How do they do it? J Biol Phys 33:345-356.
    • (2007) J Biol Phys , vol.33 , pp. 345-356
    • Herce, H.1    Garcia, A.2
  • 16
    • 79851511792 scopus 로고    scopus 로고
    • Targeting pathways of c-tail-anchored proteins
    • Borgese N, Fasana E (2011) Targeting pathways of c-tail-anchored proteins. Biochim Biophys Acta 1808: 937-946.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 937-946
    • Borgese, N.1    Fasana, E.2
  • 17
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • Hegde R, Keenan R (2011) Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat Rev Mol Cell Biol 12:787-798.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 787-798
    • Hegde, R.1    Keenan, R.2
  • 18
    • 79955650131 scopus 로고    scopus 로고
    • A look at arginine in membranes
    • Hristova K, Wimley W (2011) A look at arginine in membranes. J Membr Biol 239:49-56.
    • (2011) J Membr Biol , vol.239 , pp. 49-56
    • Hristova, K.1    Wimley, W.2
  • 19
    • 78649770531 scopus 로고    scopus 로고
    • Why are polar residues within the membrane core evolutionary conserved?
    • Illergard K, Kauko A, Elofsson A (2011) Why are polar residues within the membrane core evolutionary conserved? Proteins 79:79-91.
    • (2011) Proteins , vol.79 , pp. 79-91
    • Illergard, K.1    Kauko, A.2    Elofsson, A.3
  • 21
    • 0034492193 scopus 로고    scopus 로고
    • Reorientation of aquaporin-1 topology during maturation in the endoplasmic reticulum
    • Lu Y, Turnbull I, Bragin A, Carveth K, Verkman A, Skach W (2000) Reorientation of aquaporin-1 topology during maturation in the endoplasmic reticulum. Mol Biol Cell 11:2973-2985.
    • (2000) Mol Biol Cell , vol.11 , pp. 2973-2985
    • Lu, Y.1    Turnbull, I.2    Bragin, A.3    Carveth, K.4    Verkman, A.5    Skach, W.6
  • 22
    • 0034602391 scopus 로고    scopus 로고
    • Identification of sequence determinants that direct different intracellular folding pathways for aquaporin-1 and aquaporin-4
    • Foster W, Helm A, Turnbull I, Gulati H, Yang B, Verkman A, Skach W (2000) Identification of sequence determinants that direct different intracellular folding pathways for aquaporin-1 and aquaporin-4. J Biol Chem 275:34157-34165.
    • (2000) J Biol Chem , vol.275 , pp. 34157-34165
    • Foster, W.1    Helm, A.2    Turnbull, I.3    Gulati, H.4    Yang, B.5    Verkman, A.6    Skach, W.7
  • 23
    • 0037177864 scopus 로고    scopus 로고
    • Evidence that the transmembrane biogenesis of aquaporin 1 is cotranslational in intact mammalian cells
    • Dohke Y, Turner R (2002) Evidence that the transmembrane biogenesis of aquaporin 1 is cotranslational in intact mammalian cells. J Biol Chem 277:15215-15219.
    • (2002) J Biol Chem , vol.277 , pp. 15215-15219
    • Dohke, Y.1    Turner, R.2
  • 24
    • 12844283314 scopus 로고    scopus 로고
    • Differential stability of biogenesis intermediates reveals a common pathway for aquaporin-1 topological maturation
    • Buck T, Skach W (2005) Differential stability of biogenesis intermediates reveals a common pathway for aquaporin-1 topological maturation. J Biol Chem 280: 261-269.
    • (2005) J Biol Chem , vol.280 , pp. 261-269
    • Buck, T.1    Skach, W.2
  • 26
    • 57349168025 scopus 로고    scopus 로고
    • Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for n(in)-c(out) and n(out)-c(in) transmembrane helices
    • Lundin C, Kim H, Nilsson I, White S, von Heijne G (2008) Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for n(in)-c(out) and n(out)-c(in) transmembrane helices. Proc Natl Acad Sci USA 105:15702-15707.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15702-15707
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.4    Von Heijne, G.5
  • 27
    • 0033601259 scopus 로고    scopus 로고
    • Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits
    • Armulik A, Nilsson I, von Heijne G, Johansson S (1999) Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J Biol Chem 274:37030-37034.
    • (1999) J Biol Chem , vol.274 , pp. 37030-37034
    • Armulik, A.1    Nilsson, I.2    Von Heijne, G.3    Johansson, S.4
  • 28
    • 10244252813 scopus 로고    scopus 로고
    • Transmembrane proteins in the protein data bank: Identification and classification
    • Tusnady G, Dosztanyi Z, Simon I (2004) Transmembrane proteins in the protein data bank: Identification and classification. Bioinformatics 20:2964-2972.
    • (2004) Bioinformatics , vol.20 , pp. 2964-2972
    • Tusnady, G.1    Dosztanyi, Z.2    Simon, I.3
  • 29
    • 34247633528 scopus 로고    scopus 로고
    • On the thermodynamic stability of a charged arginine side chain in a transmembrane helix
    • Dorairaj S, Allen T (2007) On the thermodynamic stability of a charged arginine side chain in a transmembrane helix. Proc Natl Acad Sci USA 104:4943-4948.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4943-4948
    • Dorairaj, S.1    Allen, T.2
  • 30
    • 79954723199 scopus 로고    scopus 로고
    • On the role of anionic lipids in charged protein interactions with membranes
    • Vorobyov I, Allen T (2011) On the role of anionic lipids in charged protein interactions with membranes. Biochim Biophys Acta 1808:1673-1683.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1673-1683
    • Vorobyov, I.1    Allen, T.2
  • 31
    • 79955654072 scopus 로고    scopus 로고
    • Arginine in membranes: The connection between molecular dynamics simulations and translocon-mediated insertion experiments
    • Schow E, Freites J, Cheng P, Bernsel A, von Heijne G, White S, Tobias D (2011) Arginine in membranes: The connection between molecular dynamics simulations and translocon-mediated insertion experiments. J Membr Biol 239:35-48.
    • (2011) J Membr Biol , vol.239 , pp. 35-48
    • Schow, E.1    Freites, J.2    Cheng, P.3    Bernsel, A.4    Von Heijne, G.5    White, S.6    Tobias, D.7
  • 32
    • 79952771298 scopus 로고    scopus 로고
    • Free-energy cost for translocon-assisted insertion of membrane proteins
    • Gumbart J, Chipot C, Schulten K (2011) Free-energy cost for translocon-assisted insertion of membrane proteins. Proc Natl Acad Sci USA 108:3596-3601.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3596-3601
    • Gumbart, J.1    Chipot, C.2    Schulten, K.3
  • 33
    • 70349436810 scopus 로고    scopus 로고
    • Protein contents in biological membranes can explain abnormal solvation of charged and polar residues
    • Johansson A, Lindahl E (2009) Protein contents in biological membranes can explain abnormal solvation of charged and polar residues. Proc Natl Acad Sci USA 106:15684-15689.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15684-15689
    • Johansson, A.1    Lindahl, E.2
  • 34
    • 78049308598 scopus 로고    scopus 로고
    • On the energetics of translocon-assisted insertion of charged transmembrane helices into membranes
    • Rychkova A, Vicatos S, Warshel A (2010) On the energetics of translocon-assisted insertion of charged transmembrane helices into membranes. Proc Natl Acad Sci USA 107:17598-17603.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17598-17603
    • Rychkova, A.1    Vicatos, S.2    Warshel, A.3
  • 35
    • 55549108720 scopus 로고    scopus 로고
    • The surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membrane
    • Martinez-Gil L, Perez-Gil J, Mingarro I (2008) The surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membrane., Biophys J 95:L36-L38.
    • (2008) Biophys J , vol.95
    • Martinez-Gil, L.1    Perez-Gil, J.2    Mingarro, I.3
  • 36
    • 0029916911 scopus 로고    scopus 로고
    • The swiss-prot protein sequence data bank and its new supplement trembl
    • Bairoch A, Apweiler R (1996) The swiss-prot protein sequence data bank and its new supplement trembl. Nucleic Acids Res 24:17-21.
    • (1996) Nucleic Acids Res , vol.24 , pp. 17-21
    • Bairoch, A.1    Apweiler, R.2
  • 37
    • 63349085641 scopus 로고    scopus 로고
    • Kalign2: High-performance multiple alignment of protein and nucleotide sequences allowing external features
    • Lassmann T, Frings O, Sonnhammer E (2009) Kalign2: High-performance multiple alignment of protein and nucleotide sequences allowing external features. Nucleic Acids Res 37:858-865.
    • (2009) Nucleic Acids Res , vol.37 , pp. 858-865
    • Lassmann, T.1    Frings, O.2    Sonnhammer, E.3
  • 38
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson M, Nilsson I, von Heijne G (1993) Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol Gen Genet 239:251-256.
    • (1993) Mol Gen Genet , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    Von Heijne, G.3
  • 39
    • 0024394362 scopus 로고
    • Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems
    • Kozak M (1989) Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems. Mol Cell Biol 9:5073-5080.
    • (1989) Mol Cell Biol , vol.9 , pp. 5073-5080
    • Kozak, M.1
  • 40
    • 0032510739 scopus 로고    scopus 로고
    • The amino acid following an asn-x-ser/thr sequon is an important determinant of n-linked core glycosylation efficiency
    • Mellquist J, Kasturi L, Spitalnik S, Shakin-Eshleman S (1998) The amino acid following an asn-x-ser/thr sequon is an important determinant of n-linked core glycosylation efficiency. Biochemistry 37:6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.1    Kasturi, L.2    Spitalnik, S.3    Shakin-Eshleman, S.4
  • 41
    • 0029916898 scopus 로고    scopus 로고
    • The amino acid at the x position of an asn-x-ser sequon is an important determinant of n-linked core-glycosylation efficiency
    • Shakin-Eshleman S, Spitalnik S, Kasturi L (1996) The amino acid at the x position of an asn-x-ser sequon is an important determinant of n-linked core-glycosylation efficiency. J Biol Chem 271:6363-6366.
    • (1996) J Biol Chem , vol.271 , pp. 6363-6366
    • Shakin-Eshleman, S.1    Spitalnik, S.2    Kasturi, L.3
  • 42
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4: Algorithms for highly efficient, loadbalanced, and scalable molecular simulation
    • doi:10.1021/ct700301q. Available at: URL arXiv
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) Gromacs 4: Algorithms for highly efficient, loadbalanced, and scalable molecular simulation, J Chem Theory Comput 4:435-447. arXiv:http://pubs.acs.org/doi/pdf/ 10.1021/ct700301q, doi:10.1021/ct700301q. Available at: URL.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 43
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jahnig F (1997) Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J 72:2002-2013.
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 44
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • Wolf MG, Hoefling M, Aponte-Santamaria C, Grubmuller H, Groenhof G (2010) G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation, J Comput Chem 31:2169-2174.
    • (2010) J Comput Chem , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaria, C.3    Grubmuller, H.4    Groenhof, G.5
  • 45
    • 78651282170 scopus 로고    scopus 로고
    • G-whamsa free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • Hub JS, de Groot BL, van der Spoel D (2010) G-whamsa free weighted histogram analysis implementation including robust error and autocorrelation estimates, J Chem Theory Comput 6:3713-3720.
    • (2010) J Chem Theory Comput , vol.6 , pp. 3713-3720
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 46
    • 84878723802 scopus 로고    scopus 로고
    • Vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein
    • Vitrac H, Bogdanov M, Dowhan W (2013) In vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein. Proc Natl Acad Sci U S A 110:9338-9343.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9338-9343
    • Vitrac, H.1    Bogdanov, M.2    Dowhan, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.