메뉴 건너뛰기




Volumn 589, Issue 24, 2015, Pages 3921-3928

Membrane insertion and topology of the amino-terminal domain TMD0 of multidrug-resistance associated protein 6 (MRP6)

Author keywords

ABCC6; ATP binding cassette transporter; Membrane protein insertion; Multidrug resistance associated protein 6; Pseudoxanthoma elasticum; Transmembrane domain

Indexed keywords

MULTIDRUG RESISTANCE ASSOCIATED PROTEIN 6; ABCC6 PROTEIN, HUMAN; MULTIDRUG RESISTANCE PROTEIN;

EID: 84959572680     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.10.030     Document Type: Article
Times cited : (19)

References (49)
  • 4
    • 0036829109 scopus 로고    scopus 로고
    • Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6)
    • M.G. Belinsky, Z.S. Chen, I. Shchaveleva, H. Zeng, G.D. Kruh, Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6). Cancer Res., 62, 21 (2002), 6172-6177.
    • (2002) Cancer Res. , vol.62 , Issue.21 , pp. 6172-6177
    • Belinsky, M.G.1    Chen, Z.S.2    Shchaveleva, I.3    Zeng, H.4    Kruh, G.D.5
  • 10
    • 78650667865 scopus 로고    scopus 로고
    • Study of the nucleotide-binding domain 1 of the human transporter protein MRP6
    • A. Ostuni, R. Miglionico, M.A. Castiglione Morelli, F. Bisaccia, Study of the nucleotide-binding domain 1 of the human transporter protein MRP6. Prot. Pept. Lett., 17, 12 (2010), 1553-1558.
    • (2010) Prot. Pept. Lett. , vol.17 , Issue.12 , pp. 1553-1558
    • Ostuni, A.1    Miglionico, R.2    Castiglione Morelli, M.A.3    Bisaccia, F.4
  • 12
    • 80052449326 scopus 로고    scopus 로고
    • Multidrug resistance proteins (MRPs/ABCCs) in cancer chemotherapy and genetic diseases
    • Z.S.S. Chen, A.K. Tiwari, Multidrug resistance proteins (MRPs/ABCCs) in cancer chemotherapy and genetic diseases. FEBS J., 278, (2011), 3226-3245.
    • (2011) FEBS J. , vol.278 , pp. 3226-3245
    • Chen, Z.S.S.1    Tiwari, A.K.2
  • 13
    • 79957737791 scopus 로고    scopus 로고
    • Mammalian peroxisomal ABC transporters: From endogenous substrates to pathology and clinical significance
    • S. Kemp, F.L. Theodoulou, R.J. Wanders, Mammalian peroxisomal ABC transporters: from endogenous substrates to pathology and clinical significance. Br. J. Pharmacol., 164, 7 (2011), 1753-1766.
    • (2011) Br. J. Pharmacol. , vol.164 , Issue.7 , pp. 1753-1766
    • Kemp, S.1    Theodoulou, F.L.2    Wanders, R.J.3
  • 14
    • 79953183131 scopus 로고    scopus 로고
    • Insights into the mechanisms underlying CFTR channel activity, the molecular basis for cystic fibrosis and strategies for therapy
    • P. Kim Chiaw, P.D. Eckford, C.E. Bear, Insights into the mechanisms underlying CFTR channel activity, the molecular basis for cystic fibrosis and strategies for therapy. Essays Biochem., 50, 1 (2011), 233-248.
    • (2011) Essays Biochem. , vol.50 , Issue.1 , pp. 233-248
    • Kim Chiaw, P.1    Eckford, P.D.2    Bear, C.E.3
  • 16
    • 0037163124 scopus 로고    scopus 로고
    • Role of the N-terminal transmembrane region of the multidrug resistance protein MRP2 in routing to the apical membrane in MDCKII cells
    • S.B. Fernández, Z. Holló, A. Kern, E. Bakos, P.A. Fischer, P. Borst, R. Evers, Role of the N-terminal transmembrane region of the multidrug resistance protein MRP2 in routing to the apical membrane in MDCKII cells. J. Biol. Chem., 277, (2002), 31048-31055.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31048-31055
    • Fernández, S.B.1    Holló, Z.2    Kern, A.3    Bakos, E.4    Fischer, P.A.5    Borst, P.6    Evers, R.7
  • 17
    • 33749354080 scopus 로고    scopus 로고
    • The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels
    • K. Fang, L. Csanády, K. Chan, The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels. J. Physiol. (Lond.), 576, (2006), 379-389.
    • (2006) J. Physiol. (Lond.) , vol.576 , pp. 379-389
    • Fang, K.1    Csanády, L.2    Chan, K.3
  • 18
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • A. Krogh, B. Larsson, G. von Heijne, E.L.L. Sonnhammer, Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol., 305, 3 (2001), 567-580.
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 19
    • 84880641715 scopus 로고    scopus 로고
    • Co-translational targeting and translocation of proteins to the endoplasmic reticulum
    • Y. Nyathi, B.M. Wilkinson, M.R. Pool, Co-translational targeting and translocation of proteins to the endoplasmic reticulum. Biochim. Biophys. Acta, 1833, (2013), 2392-2402.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2392-2402
    • Nyathi, Y.1    Wilkinson, B.M.2    Pool, M.R.3
  • 20
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport, Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature, 450, (2007), 663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 21
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • S. Shao, R.S. Hegde, Membrane protein insertion at the endoplasmic reticulum. Annu. Rev. Cell Dev. Biol., 27, (2011), 25-56.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 23
    • 0024394362 scopus 로고
    • Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems
    • M. Kozak, Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems. Mol. Cell. Biol., 9, (1989), 5073-5080.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5073-5080
    • Kozak, M.1
  • 25
    • 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
    • M. Johansson, I. Nilsson, G. von Heijne, 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, (1993), 251-256.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    Von Heijne, G.3
  • 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
    • C. Lundin, H. Kim, I. Nilsson, S.H. White, G. von Heijne, 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. U.S.A., 105, (2008), 15702-15707.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15702-15707
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.H.4    Von Heijne, G.5
  • 28
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • P. Walter, G. Blobel, Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol., 96, (1983), 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 30
    • 84857439394 scopus 로고    scopus 로고
    • Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix
    • K. Öjemalm, K.K. Halling, I. Nilsson, G. von Heijne, Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix. Mol. Cell, 45, 4 (2012), 529-540.
    • (2012) Mol. Cell , vol.45 , Issue.4 , pp. 529-540
    • Öjemalm, K.1    Halling, K.K.2    Nilsson, I.3    Von Heijne, G.4
  • 31
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T. Nordahl Petersen, S. Brunak, G. von Heijne, H. Nielsen, SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods, 8, (2011), 785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Nordahl Petersen, T.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 32
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • R. Daniels, B. Kurowski, A.E. Johnson, D.N. Hebert, N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell, 11, (2003), 79-90.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 33
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • I. Nilsson, P. Whitley, G. von Heijne, The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol., 126, (1994), 1127-1132.
    • (1994) J. Cell Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    Von Heijne, G.3
  • 34
    • 84899823053 scopus 로고    scopus 로고
    • Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations
    • J. Wanngren, P. Lara, K. Ojemalm, S. Maioli, N. Moradi, L. Chen, L.O. Tjernberg, J. Lundkvist, I. Nilsson, H. Karlström, Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations. FEBS Open Bio, 4, (2014), 393-406.
    • (2014) FEBS Open Bio , vol.4 , pp. 393-406
    • Wanngren, J.1    Lara, P.2    Ojemalm, K.3    Maioli, S.4    Moradi, N.5    Chen, L.6    Tjernberg, L.O.7    Lundkvist, J.8    Nilsson, I.9    Karlström, H.10
  • 35
    • 0035951866 scopus 로고    scopus 로고
    • Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum
    • X. Chen, C. Van Valkenburgh, H. Liang, H. Fang, N. Green, Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum. J. Biol. Chem., 276, (2001), 2411-2416.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2411-2416
    • Chen, X.1    Van Valkenburgh, C.2    Liang, H.3    Fang, H.4    Green, N.5
  • 37
    • 0025630756 scopus 로고
    • Residues flanking the COOH-terminal C-region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase and the extent of coupling of its co-translational translocation and proteolytic processing in vitro
    • S.F. Nothwehr, S.D. Hoeltzli, K.L. Allen, M.O. Lively, J.I. Gordon, Residues flanking the COOH-terminal C-region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase and the extent of coupling of its co-translational translocation and proteolytic processing in vitro. J. Biol. Chem., 265, (1990), 21797-21803.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21797-21803
    • Nothwehr, S.F.1    Hoeltzli, S.D.2    Allen, K.L.3    Lively, M.O.4    Gordon, J.I.5
  • 38
    • 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
    • J.L. Mellquist, L. Kasturi, S.L. Spitalnik, S.H. Shakin-Eshleman, The amino acid following an asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency. Biochemistry, 37, (1998), 6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.L.1    Kasturi, L.2    Spitalnik, S.L.3    Shakin-Eshleman, S.H.4
  • 39
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • L. Kasturi, J.R. Eshleman, W.H. Wunner, S.H. Shakin-Eshleman, The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J. Biol. Chem., 270, (1995), 14756-14761.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.R.2    Wunner, W.H.3    Shakin-Eshleman, S.H.4
  • 40
    • 78650799822 scopus 로고    scopus 로고
    • N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon
    • M. Bañó-Polo, F. Baldin, S. Tamborero, M.A. Marti-Renom, I. Mingarro, N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon. Protein Sci., 20, (2011), 179-186.
    • (2011) Protein Sci. , vol.20 , pp. 179-186
    • Bañó-Polo, M.1    Baldin, F.2    Tamborero, S.3    Marti-Renom, M.A.4    Mingarro, I.5
  • 43
    • 0034815179 scopus 로고    scopus 로고
    • Identification of ABCC6 pseudogenes on human chromosome 16p: Implications for mutation detection in pseudoxanthoma elasticum
    • L. Pulkkinen, A. Nakano, F. Ringpfeil, J. Uitto, Identification of ABCC6 pseudogenes on human chromosome 16p: implications for mutation detection in pseudoxanthoma elasticum. Hum. Genet., 109, (2001), 356-365.
    • (2001) Hum. Genet. , vol.109 , pp. 356-365
    • Pulkkinen, L.1    Nakano, A.2    Ringpfeil, F.3    Uitto, J.4
  • 44
    • 38849135998 scopus 로고    scopus 로고
    • Novel clinic-molecular insights in pseudoxanthoma elasticum provide an efficient molecular screening method and a comprehensive diagnostic flowchart
    • O. Vanakker, B. Leroy, P. Coucke, L. Bercovitch, J. Uitto, D. Viljoen, S. Terry, P. Acker, D. Matthys, B. Loeys, A. Paepe, Novel clinic-molecular insights in pseudoxanthoma elasticum provide an efficient molecular screening method and a comprehensive diagnostic flowchart. Hum. Mutat., 29, (2008), 205 -
    • (2008) Hum. Mutat. , vol.29 , pp. 205
    • Vanakker, O.1    Leroy, B.2    Coucke, P.3    Bercovitch, L.4    Uitto, J.5    Viljoen, D.6    Terry, S.7    Acker, P.8    Matthys, D.9    Loeys, B.10    Paepe, A.11
  • 47
    • 84946032322 scopus 로고    scopus 로고
    • Marginally hydrophobic transmembrane α-helices shaping membrane protein folding
    • M.T. De Marothy, A. Elofsson, Marginally hydrophobic transmembrane α-helices shaping membrane protein folding. Protein Sci., 24, (2015), 1057-1074.
    • (2015) Protein Sci. , vol.24 , pp. 1057-1074
    • De Marothy, M.T.1    Elofsson, A.2
  • 48
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • G. von Heijne, The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J., 5, (1986), 3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 49
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • G. von Heijne, Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature, 341, (1989), 456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.