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Volumn 585, Issue 3, 2011, Pages 517-522

Protein N-acylation overrides differing targeting signals

Author keywords

Calcium dependent protein kinase; Chloroplast targeting; Myristoylation; Palmitoylation; Protein kinase

Indexed keywords

ALANINE; CALPAIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; GLYCINE; PROLINE; PROTEIN KINASE; PROTEIN KINASE KIN1; PROTEIN KINASE KIN2; PROTEIN KINASE KIN3; PROTEIN KINASE KIN4; PROTEIN SERINE THREONINE KINASE; RIBULOSEBISPHOSPHATE CARBOXYLASE; SERINE; THREONINE TRANSFER RNA LIGASE; UNCLASSIFIED DRUG;

EID: 79551485462     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.01.001     Document Type: Article
Times cited : (45)

References (35)
  • 2
    • 33845874376 scopus 로고    scopus 로고
    • Compartmentation in plant metabolism
    • J.E. Lunn Compartmentation in plant metabolism J. Exp. Bot. 58 2007 35 47
    • (2007) J. Exp. Bot. , vol.58 , pp. 35-47
    • Lunn, J.E.1
  • 3
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • G. Blobel Intracellular protein topogenesis Proc. Natl. Acad. Sci. USA 77 1980 1496 1500
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 4
    • 0019881130 scopus 로고
    • On the hydrophobic nature of signal sequences
    • G. von Heijne On the hydrophobic nature of signal sequences Eur. J. Biochem. 116 1981 419 422
    • (1981) Eur. J. Biochem. , vol.116 , pp. 419-422
    • Von Heijne, G.1
  • 6
    • 0041876303 scopus 로고    scopus 로고
    • Membrane proteins - Introduction
    • J.H. Kleinschmidt Membrane proteins - introduction Cell. Mol. Life Sci. 60 2003 1527 1528
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1527-1528
    • Kleinschmidt, J.H.1
  • 8
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • F.L. Zhang, and P.J. Casey Protein prenylation: molecular mechanisms and functional consequences Annu. Rev. Biochem. 65 1996 241 269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 10
    • 0033552652 scopus 로고    scopus 로고
    • Protein myristoylation in protein-lipid and protein-protein interactions
    • H. Taniguchi Protein myristoylation in protein-lipid and protein-protein interactions Biophys. Chem. 82 1999 129 137
    • (1999) Biophys. Chem. , vol.82 , pp. 129-137
    • Taniguchi, H.1
  • 12
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • T.A. Farazi, G. Waksman, and J.I. Gordon The biology and enzymology of protein N-myristoylation J. Biol. Chem. 276 2001 39501 39504
    • (2001) J. Biol. Chem. , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 13
    • 70450188170 scopus 로고    scopus 로고
    • Protein lipid modifications in signaling and subcellular targeting
    • N. Sorek, D. Bloch, and S. Yalovsky Protein lipid modifications in signaling and subcellular targeting Curr. Opin. Plant Biol. 12 2009 714 720
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 714-720
    • Sorek, N.1    Bloch, D.2    Yalovsky, S.3
  • 14
    • 0036290648 scopus 로고    scopus 로고
    • N-Terminal N-myristoylation of proteins: Prediction of substrate proteins from amino acid sequence
    • S. Maurer-Stroh, B. Eisenhaber, and F. Eisenhaber N-Terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence J. Mol. Biol. 317 2002 541 557
    • (2002) J. Mol. Biol. , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 15
    • 2942564436 scopus 로고    scopus 로고
    • N-Terminal myristoylation predictions by ensembles of neural networks
    • G. Bologna, C. Yvon, S. Duvaud, and A.L. Veuthey N-Terminal myristoylation predictions by ensembles of neural networks Proteomics 4 2004 1626 1632
    • (2004) Proteomics , vol.4 , pp. 1626-1632
    • Bologna, G.1    Yvon, C.2    Duvaud, S.3    Veuthey, A.L.4
  • 16
    • 9144256852 scopus 로고    scopus 로고
    • Predicting N-terminal myristoylation sites in plant proteins
    • S. Podell, and M. Gribskov Predicting N-terminal myristoylation sites in plant proteins BMC Genomics 5 2004 37
    • (2004) BMC Genomics , vol.5 , pp. 37
    • Podell, S.1    Gribskov, M.2
  • 17
  • 19
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • R.M. Peitzsch, and S. McLaughlin Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins Biochemistry 32 1993 10436 10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 20
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • D. Murray, N. Ben-Tal, B. Honig, and S. McLaughlin Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology Structure 5 1997 985 989
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 23
    • 0033793156 scopus 로고    scopus 로고
    • SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding
    • M. Ishitani, J. Liu, U. Halfter, C.S. Kim, W. Shi, and J.K. Zhu SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding Plant Cell 12 2000 1667 1678
    • (2000) Plant Cell , vol.12 , pp. 1667-1678
    • Ishitani, M.1    Liu, J.2    Halfter, U.3    Kim, C.S.4    Shi, W.5    Zhu, J.K.6
  • 24
    • 0037062514 scopus 로고    scopus 로고
    • Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3
    • Q.S. Qiu, Y. Guo, M.A. Dietrich, K.S. Schumaker, and J.K. Zhu Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3 Proc. Natl. Acad. Sci. USA 99 2002 8436 8441
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8436-8441
    • Qiu, Q.S.1    Guo, Y.2    Dietrich, M.A.3    Schumaker, K.S.4    Zhu, J.K.5
  • 25
    • 14744271077 scopus 로고    scopus 로고
    • N-Myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning
    • S. Colombo, R. Longhi, S. Alcaro, F. Ortuso, T. Sprocati, A. Flora, and N. Borgese N-Myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning J. Cell Biol. 168 2005 735 745
    • (2005) J. Cell Biol. , vol.168 , pp. 735-745
    • Colombo, S.1    Longhi, R.2    Alcaro, S.3    Ortuso, F.4    Sprocati, T.5    Flora, A.6    Borgese, N.7
  • 26
    • 0025813516 scopus 로고
    • A strategy for efficient in vitro translation of cDNAs using the rabbit beta-globin leader sequence
    • A. Annweiler, R.A. Hipskind, and T. Wirth A strategy for efficient in vitro translation of cDNAs using the rabbit beta-globin leader sequence Nucleic Acids Res. 19 1991 3750
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3750
    • Annweiler, A.1    Hipskind, R.A.2    Wirth, T.3
  • 27
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • M. Bevan Binary Agrobacterium vectors for plant transformation Nucleic Acids Res. 12 1984 8711 8721
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 28
    • 57349084079 scopus 로고    scopus 로고
    • Experimental testing of predicted myristoylation targets involved in asymmetric cell division and calcium-dependent signalling
    • W. Benetka Experimental testing of predicted myristoylation targets involved in asymmetric cell division and calcium-dependent signalling Cell Cycle 7 2008 3709 3719
    • (2008) Cell Cycle , vol.7 , pp. 3709-3719
    • Benetka, W.1
  • 31
    • 46049104182 scopus 로고    scopus 로고
    • A survey of chloroplast protein kinases and phosphatases in Arabidopsis thaliana
    • I. Schliebner, M. Pribil, J. Zuhlke, A. Dietzmann, and D. Leister A survey of chloroplast protein kinases and phosphatases in Arabidopsis thaliana Curr. Genomics 9 2008 184 190
    • (2008) Curr. Genomics , vol.9 , pp. 184-190
    • Schliebner, I.1    Pribil, M.2    Zuhlke, J.3    Dietzmann, A.4    Leister, D.5
  • 34
    • 28044436758 scopus 로고    scopus 로고
    • Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana
    • A.M. Duchene Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana Proc. Natl. Acad. Sci. USA 102 2005 16484 16489
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16484-16489
    • Duchene, A.M.1
  • 35
    • 34247562746 scopus 로고    scopus 로고
    • How can organellar protein N-terminal sequences be dual targeting signals? in silico analysis and mutagenesis approach
    • C. Pujol, L. Marechal-Drouard, and A.M. Duchene How can organellar protein N-terminal sequences be dual targeting signals? In silico analysis and mutagenesis approach J. Mol. Biol. 369 2007 356 367
    • (2007) J. Mol. Biol. , vol.369 , pp. 356-367
    • Pujol, C.1    Marechal-Drouard, L.2    Duchene, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.