메뉴 건너뛰기




Volumn 582, Issue 6, 2008, Pages 855-860

The outer membrane form of the mitochondrial protein Mcr1 follows a TOM-independent membrane insertion pathway

Author keywords

Mcr1; Mitochondria; Outer membrane; Protein import; Signal anchored protein

Indexed keywords

CARRIER PROTEIN; FUNGAL PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN MCR1; UNCLASSIFIED DRUG;

EID: 40149096482     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.02.009     Document Type: Article
Times cited : (38)

References (24)
  • 1
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • W. Neupert Protein import into mitochondria Annu. Rev. Biochem. 66 1997 863 917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 2
    • 20044387943 scopus 로고    scopus 로고
    • Single translation–dual destination: mechanisms of dual protein targeting in eukaryotes
    • S. Karniely O. Pines Single translation–dual destination: mechanisms of dual protein targeting in eukaryotes EMBO Rep. 6 2005 420 425
    • (2005) EMBO Rep. , vol.6 , pp. 420-425
    • Karniely, S.1    Pines, O.2
  • 3
    • 0027940215 scopus 로고
    • Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments
    • K. Hahne V. Haucke L. Ramage G. Schatz Incomplete arrest in the outer membrane sorts NADH-cytochrome b 5 reductase to two different submitochondrial compartments Cell 79 1994 829 839
    • (1994) Cell , vol.79 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Ramage, L.3    Schatz, G.4
  • 4
    • 0030982770 scopus 로고    scopus 로고
    • Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria
    • V. Haucke C.S. Ocana A. Honlinger K. Tokatlidis N. Pfanner G. Schatz Analysis of the sorting signals directing NADH-cytochrome b 5 reductase to two locations within yeast mitochondria Mol. Cell. Biol. 17 1997 4024 4032
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4024-4032
    • Haucke, V.1    Ocana, C.S.2    Honlinger, A.3    Tokatlidis, K.4    Pfanner, N.5    Schatz, G.6
  • 6
    • 0242607644 scopus 로고    scopus 로고
    • How to find the right organelle – targeting signals in mitochondrial outer membrane proteins
    • D. Rapaport How to find the right organelle – targeting signals in mitochondrial outer membrane proteins EMBO Rep. 4 2003 948 952
    • (2003) EMBO Rep. , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 7
    • 12844276571 scopus 로고    scopus 로고
    • Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria
    • U. Ahting T. Waizenegger W. Neupert D. Rapaport Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria J. Biol. Chem. 280 2005 48 53
    • (2005) J. Biol. Chem. , vol.280 , pp. 48-53
    • Ahting, U.1    Waizenegger, T.2    Neupert, W.3    Rapaport, D.4
  • 8
    • 0028239372 scopus 로고
    • Yeast mitochondria lacking the two import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins
    • T. Lithgow T. Junne C. Wachter G. Schatz Yeast mitochondria lacking the two import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins J. Biol. Chem. 269 1994 15325 15330
    • (1994) J. Biol. Chem. , vol.269 , pp. 15325-15330
    • Lithgow, T.1    Junne, T.2    Wachter, C.3    Schatz, G.4
  • 9
    • 0027186299 scopus 로고
    • Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex
    • C.K. Kassenbrock W. Cao M.G. Douglas Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex EMBO J. 12 1993 3023 3034
    • (1993) EMBO J. , vol.12 , pp. 3023-3034
    • Kassenbrock, C.K.1    Cao, W.2    Douglas, M.G.3
  • 10
    • 0020479721 scopus 로고
    • Import of proteins into mitochondria: energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria
    • 2 by isolated yeast mitochondria J. Biol. Chem. 257 1982 13075 13080
    • (1982) J. Biol. Chem. , vol.257 , pp. 13075-13080
    • Daum, G.1    Gasser, S.2    Schatz, G.3
  • 11
    • 2442551481 scopus 로고    scopus 로고
    • During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria
    • P.K. Kim M.G. Annis P.J. Dlugosz B. Leber D.W. Andrews During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria Mol. Cell 14 2004 523 529
    • (2004) Mol. Cell , vol.14 , pp. 523-529
    • Kim, P.K.1    Annis, M.G.2    Dlugosz, P.J.3    Leber, B.4    Andrews, D.W.5
  • 12
    • 0027939249 scopus 로고
    • Surface labelling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin
    • M. Krishnasastry B. Walker O. Braha H. Bayley Surface labelling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin FEBS Lett. 356 1994 66 71
    • (1994) FEBS Lett. , vol.356 , pp. 66-71
    • Krishnasastry, M.1    Walker, B.2    Braha, O.3    Bayley, H.4
  • 13
    • 0035931764 scopus 로고    scopus 로고
    • Biogenesis of the major mitochondrial outer membrane protein porin involves a complex import pathway via receptors and the general import pore
    • T. Krimmer Biogenesis of the major mitochondrial outer membrane protein porin involves a complex import pathway via receptors and the general import pore J. Cell Biol. 152 2001 289 300
    • (2001) J. Cell Biol. , vol.152 , pp. 289-300
    • Krimmer, T.1
  • 14
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins of mitochondria
    • S.A. Paschen W. Neupert D. Rapaport Biogenesis of beta-barrel membrane proteins of mitochondria Trends Biochem. Sci. 30 2005 575 582
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 15
    • 30844449228 scopus 로고    scopus 로고
    • Chaperoning through the mitochondrial intermembrane space
    • N. Wiedemann N. Pfanner A. Chacinska Chaperoning through the mitochondrial intermembrane space Mol. Cell 21 2006 145 148
    • (2006) Mol. Cell , vol.21 , pp. 145-148
    • Wiedemann, N.1    Pfanner, N.2    Chacinska, A.3
  • 17
    • 0033620612 scopus 로고    scopus 로고
    • Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20
    • E. Schleiff J.R. Silvius G.C. Shore Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20 J. Cell Biol. 145 1999 973 978
    • (1999) J. Cell Biol. , vol.145 , pp. 973-978
    • Schleiff, E.1    Silvius, J.R.2    Shore, G.C.3
  • 18
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • G. Von Heijne Mitochondrial targeting sequences may form amphiphilic helices EMBO J. 5 1986 1335 1342
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 19
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • W. Neupert J.M. Herrmann Translocation of proteins into mitochondria Annu. Rev. Biochem. 76 2007 723 749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 20
    • 0142242210 scopus 로고    scopus 로고
    • Signal-anchor domains of proteins of the outer membrane of mitochondria: structural and functional characteristics
    • T. Waizenegger T. Stan W. Neupert D. Rapaport Signal-anchor domains of proteins of the outer membrane of mitochondria: structural and functional characteristics J. Biol. Chem. 278 2003 42064 42071
    • (2003) J. Biol. Chem. , vol.278 , pp. 42064-42071
    • Waizenegger, T.1    Stan, T.2    Neupert, W.3    Rapaport, D.4
  • 21
    • 27744543167 scopus 로고    scopus 로고
    • How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
    • D. Rapaport How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane? J. Cell Biol. 171 2005 419 423
    • (2005) J. Cell Biol. , vol.171 , pp. 419-423
    • Rapaport, D.1
  • 22
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • K. Setoguchi H. Otera K. Mihara Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins EMBO J. 25 2006 5635 5647
    • (2006) EMBO J. , vol.25 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 23
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • K. Gabriel B. Egan T. Lithgow Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins EMBO J. 22 2003 2380 2386
    • (2003) EMBO J. , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 24
    • 38649109133 scopus 로고    scopus 로고
    • Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane
    • J. Popov-Čeleketić T. Waizenegger D. Rapaport Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane J. Mol. Biol. 376 2008 671 680
    • (2008) J. Mol. Biol. , vol.376 , pp. 671-680
    • Popov-Čeleketić, J.1    Waizenegger, T.2    Rapaport, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.