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Volumn 119, Issue 8, 2006, Pages 1558-1569

Erratum: N-terminal palmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways (Journal of Cell Science DOI: 10.1242/jcs.02878);N-terminal palmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways

Author keywords

Caveolae; Nitric oxide; NOS2; Palmitoylation

Indexed keywords

AMINO ACID; CYSTEINE; NITRIC OXIDE SYNTHASE; PALMITIC ACID; SERINE;

EID: 33646675624     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/JCS.219675     Document Type: Erratum
Times cited : (17)

References (43)
  • 1
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M. J. and Marsh, M. (2003). The on-off story of protein palmitoylation. Trends Cell Biol. 13, 32-42.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 2
    • 0029671096 scopus 로고    scopus 로고
    • Intra-Golgi transport inhibition by megalomicin
    • Bonay, F., Munro, S., Fresno, M. and Alarcon, B. (1996). Intra-Golgi transport inhibition by megalomicin. J. Biol. Chem. 271, 3719-3726.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3719-3726
    • Bonay, F.1    Munro, S.2    Fresno, M.3    Alarcon, B.4
  • 3
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman, J. E., Chao, D. S., Xia, H., Aldape, K. and Bredt, D. S. (1995). Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82, 743-752.
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 4
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1 -syntrophin mediated by PDZ domains
    • Brenman, J. E., Chao, D. S., Gee, S. H., McGee, A. W, Craven, S. E., Santillano, D. R., Wu, Z., Huang, F., Xia, H., Peters, M. F. et al. (1996). Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1 -syntrophin mediated by PDZ domains. Cell 84, 757-767.
    • (1996) Cell , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Santillano, D.R.6    Wu, Z.7    Huang, F.8    Xia, H.9    Peters, M.F.10
  • 5
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey, P. J. (1995). Protein lipidation in cell signaling. Science 268, 221-225.
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 6
    • 0042386445 scopus 로고    scopus 로고
    • Lipid- and protein-mediated multimerization of PSD-95: Implications for receptor clustering and assembly of synaptic protein networks
    • Christopherson, K. S., Sweeney, N. T., Craven, S. E., Kang, R., El-Husseini, A. E. and Bredt, D. S. (2003). Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks. J. Cell Sci. 116, 3213-3219.
    • (2003) J. Cell Sci. , vol.116 , pp. 3213-3219
    • Christopherson, K.S.1    Sweeney, N.T.2    Craven, S.E.3    Kang, R.4    El-Husseini, A.E.5    Bredt, D.S.6
  • 7
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J. and Tainer, J. A. (1998). Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 279, 2121-2126.
    • (1998) Science , vol.279 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3    Wu, C.4    Getzoff, E.D.5    Stuehr, D.J.6    Tainer, J.A.7
  • 8
    • 10044268365 scopus 로고    scopus 로고
    • On the mechanism of protein palmitoylation
    • Dietrich, L. E. and Ungermann, C. (2004). On the mechanism of protein palmitoylation. EMBO Rep. 5, 1053-1057.
    • (2004) EMBO Rep. , vol.5 , pp. 1053-1057
    • Dietrich, L.E.1    Ungermann, C.2
  • 9
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • Dunphy, J. T. and Linder, M. E. (1998). Signalling functions of protein palmitoylation. Biochim. Biophys. Acta 1436, 245-261.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 10
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • Dunphy, J. T., Greentree, W. K., Manahan, C. L. and Linder, M. E. (1996). G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271, 7154-7159.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7154-7159
    • Dunphy, J.T.1    Greentree, W.K.2    Manahan, C.L.3    Linder, M.E.4
  • 11
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • El-Husseini, A. E., Craven, S. E., Chetkovich, D. M., Firestein, B. L., Schnell, E., Aoki, C. and Bredt, D. S. (2000). Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J. Cell Biol. 148, 159-172.
    • (2000) J. Cell Biol. , vol.148 , pp. 159-172
    • El-Husseini, A.E.1    Craven, S.E.2    Chetkovich, D.M.3    Firestein, B.L.4    Schnell, E.5    Aoki, C.6    Bredt, D.S.7
  • 12
    • 0034687690 scopus 로고    scopus 로고
    • Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells
    • Felley-Bosco, E., Bender, F. C., Courjault-Gautier, F., Bron, C. and Quest, A. F. (2000). Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells. Proc. Natl. Acad. Sci. USA 97, 14334-14339.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14334-14339
    • Felley-Bosco, E.1    Bender, F.C.2    Courjault-Gautier, F.3    Bron, C.4    Quest, A.F.5
  • 13
    • 0032488818 scopus 로고    scopus 로고
    • The endothelial nitric-oxide synthase-caveolin regulatory cycle
    • Feron, O., Saldana, F., Michel, J. B. and Michel, T. (1998). The endothelial nitric-oxide synthase-caveolin regulatory cycle. J. Biol. Chem. 273, 3125-3128.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3125-3128
    • Feron, O.1    Saldana, F.2    Michel, J.B.3    Michel, T.4
  • 14
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo
    • García-Cardena, G., Martasek, P., Masters, B. S., Skidd, P. M., Couet, J., Li, S., Lisanti, M. P. and Sessa, W. C. (1997). Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo. J. Biol. Chem. 272, 25437-25440.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25437-25440
    • García-Cardena, G.1    Martasek, P.2    Masters, B.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6    Lisanti, M.P.7    Sessa, W.C.8
  • 15
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo, S. and Linder, M. E. (1998). SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol. Biol. Cell 9, 585-597.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 16
    • 0020611667 scopus 로고
    • Dissection of the Golgi complex. I. Monensin inhibits the transport of viral membrane proteins from medial to trans Golgi cisternae in baby hamster kidney cells infected with Semliki Forest virus
    • Griffiths, G., Quinn, F. and Warren, G. (1983). Dissection of the Golgi complex. I. Monensin inhibits the transport of viral membrane proteins from medial to trans Golgi cisternae in baby hamster kidney cells infected with Semliki Forest virus. J. Cell Biol. 96, 835-850.
    • (1983) J. Cell Biol. , vol.96 , pp. 835-850
    • Griffiths, G.1    Quinn, F.2    Warren, G.3
  • 17
    • 17844378983 scopus 로고    scopus 로고
    • The human Kvl.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence
    • Gubitosi-Klug, R. A., Mancuso, D. J. and Gross, R. W. (2005). The human Kvl.1 channel is palmitoylated, modulating voltage sensing: identification of a palmitoylation consensus sequence. Proc. Natl. Acad. Sci. USA 102, 5964-5968.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5964-5968
    • Gubitosi-Klug, R.A.1    Mancuso, D.J.2    Gross, R.W.3
  • 18
    • 0027759805 scopus 로고
    • Neuronal growth cone collapse and inhibition of protein fatty acylation by nitric oxide
    • Hess, D. T., Patterson, S. I., Smith, D. S. and Skene, J. H. (1993). Neuronal growth cone collapse and inhibition of protein fatty acylation by nitric oxide. Nature 366, 562-565.
    • (1993) Nature , vol.366 , pp. 562-565
    • Hess, D.T.1    Patterson, S.I.2    Smith, D.S.3    Skene, J.H.4
  • 19
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Hsueh, Y. P., Kim, E. and Sheng, M. (1997). Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95. Neuron 18, 803-814.
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh, Y.P.1    Kim, E.2    Sheng, M.3
  • 20
    • 0025306167 scopus 로고
    • Fatty acylated proteins as components of intracellular signaling pathways
    • James, G. and Olson, E. N. (1990). Fatty acylated proteins as components of intracellular signaling pathways. Biochemistry 29, 2623-2634.
    • (1990) Biochemistry , vol.29 , pp. 2623-2634
    • James, G.1    Olson, E.N.2
  • 21
    • 0029125762 scopus 로고
    • Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer
    • Klatt, P., Schmidt, K., Lehner, D., Glatter, O., Bachinger, H. P. and Mayer, B. (1995). Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. EMBO J. 14, 3687-3695.
    • (1995) EMBO J. , vol.14 , pp. 3687-3695
    • Klatt, P.1    Schmidt, K.2    Lehner, D.3    Glatter, O.4    Bachinger, H.P.5    Mayer, B.6
  • 22
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and orgarrelle structure
    • Klausner, R. D., Donaldson, J. G. and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and orgarrelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 23
    • 0032619824 scopus 로고    scopus 로고
    • Purification of caveolae-derived membrane microdomains containing lipid-anchored signaling molecules, such as GPI-anchored proteins, H-Ras, Sre-family tyrosine kinases, eNOS, and G-protein alpha-, beta-, and gamma-subunits
    • Lisanti, M. P., Sargiacomo, M. and Scherer, P. E. (1999). Purification of caveolae-derived membrane microdomains containing lipid-anchored signaling molecules, such as GPI-anchored proteins, H-Ras, Sre-family tyrosine kinases, eNOS, and G-protein alpha-, beta-, and gamma-subunits. Methods Mol. Biol. 116, 51-60.
    • (1999) Methods Mol. Biol. , vol.116 , pp. 51-60
    • Lisanti, M.P.1    Sargiacomo, M.2    Scherer, P.E.3
  • 24
    • 0029847608 scopus 로고    scopus 로고
    • Palmitoylation of endothelial nitric oxide synthase is necessary for optimal stimulated release of nitric oxide: Implications for caveolae localization
    • Liu, J., Garcia-Cardena, G. and Sessa, W. C. (1996). Palmitoylation of endothelial nitric oxide synthase is necessary for optimal stimulated release of nitric oxide: implications for caveolae localization. Biochemistry 35, 13277-13281.
    • (1996) Biochemistry , vol.35 , pp. 13277-13281
    • Liu, J.1    Garcia-Cardena, G.2    Sessa, W.C.3
  • 25
    • 0030920365 scopus 로고    scopus 로고
    • The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: A green fluorescent protein study
    • Liu, J., Hughes, T. E. and Sessa, W. C. (1997). The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study. J. Cell Biol. 137, 1525-1535.
    • (1997) J. Cell Biol. , vol.137 , pp. 1525-1535
    • Liu, J.1    Hughes, T.E.2    Sessa, W.C.3
  • 26
    • 0642306909 scopus 로고    scopus 로고
    • Are prenyl groups on proteins sticky fingers or greasy handles?
    • Magee, A. I. and Seabra, M. C. (2003). Are prenyl groups on proteins sticky fingers or greasy handles? Biochem. J. 376, e3-e4.
    • (2003) Biochem. J. , vol.376
    • Magee, A.I.1    Seabra, M.C.2
  • 27
    • 0035200238 scopus 로고    scopus 로고
    • N-terminal protein acylation confers localization to cholesterol, sphingolipid-enriched membranes but not to lipid rafts/caveolae
    • McCabe, J. B. and Berthiaume, L. G. (2001). N-terminal protein acylation confers localization to cholesterol, sphingolipid-enriched membranes but not to lipid rafts/caveolae. Mol. Biol. Cell 12, 3601-3617.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3601-3617
    • McCabe, J.B.1    Berthiaume, L.G.2
  • 28
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan, G., Parenti, M. and Magee, A. I. (1995). The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20, 181-187.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181-187
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 29
    • 0036676541 scopus 로고    scopus 로고
    • Distance-dependent cellular palmitoylation of de-novo-designed sequences and their translocation to plasma membrane subdomains
    • Navarro-Lérida, I., Alvarez-Barrientos, A., Gavilanes, F. and Rodríguez-Crespo, I. (2002). Distance-dependent cellular palmitoylation of de-novo-designed sequences and their translocation to plasma membrane subdomains. J. Cell Sci. 115, 3119-3130.
    • (2002) J. Cell Sci. , vol.115 , pp. 3119-3130
    • Navarro-Lérida, I.1    Alvarez-Barrientos, A.2    Gavilanes, F.3    Rodríguez-Crespo, I.4
  • 30
    • 11244352052 scopus 로고    scopus 로고
    • Palmitoylation of inducible nitric-oxide synthase at Cys-3 is required for proper intracellular traffic and nitric oxide synthesis
    • Navarro-Lérida, I., Corvi, M. M., Alvarez-Barrientos, A., Gavilanes, F., Berthiaume, L. G. and Rodríguez-Crespo, I. (2004a). Palmitoylation of inducible nitric-oxide synthase at Cys-3 is required for proper intracellular traffic and nitric oxide synthesis. J. Biol. Chem. 279, 55682-55689.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55682-55689
    • Navarro-Lérida, I.1    Corvi, M.M.2    Alvarez-Barrientos, A.3    Gavilanes, F.4    Berthiaume, L.G.5    Rodríguez-Crespo, I.6
  • 32
    • 0032489512 scopus 로고    scopus 로고
    • Electron transfer and catalytic activity of nitric oxide synthases. Chimeric constructs of the neuronal, inducible, and endothelial isoforms
    • Nishida, C. R. and Ortiz de Montellano, P. R. (1998). Electron transfer and catalytic activity of nitric oxide synthases. Chimeric constructs of the neuronal, inducible, and endothelial isoforms. J. Biol. Chem. 273, 5566-5571.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5566-5571
    • Nishida, C.R.1    Ortiz de Montellano, P.R.2
  • 33
    • 0032545181 scopus 로고    scopus 로고
    • The N-terminal PDZ-containing region of postsynaptic density-95 mediates association with caveolar-like lipid domains
    • Perez, A. S. and Bredt, D. S. (1998). The N-terminal PDZ-containing region of postsynaptic density-95 mediates association with caveolar-like lipid domains. Neurosci. Lett. 258, 121-123.
    • (1998) Neurosci. Lett. , vol.258 , pp. 121-123
    • Perez, A.S.1    Bredt, D.S.2
  • 34
    • 0033569879 scopus 로고    scopus 로고
    • An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity
    • Ratovitski, E. A., Bao, C., Quick, R. A., McMillan, A., Kozlovsky, C. and Lowenstein, C. J. (1999a). An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity. J. Biol. Chem. 274, 30250-30257.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30250-30257
    • Ratovitski, E.A.1    Bao, C.2    Quick, R.A.3    McMillan, A.4    Kozlovsky, C.5    Lowenstein, C.J.6
  • 36
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 37
    • 0029889353 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation
    • Rodríguez-Crespo, I., Gerber, N. C. and Ortiz de Montellano, P. R. (1996a). Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation. J. Biol. Chem. 271, 11462-11467.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11462-11467
    • Rodríguez-Crespo, I.1    Gerber, N.C.2    Ortiz de Montellano, P.R.3
  • 38
    • 0030446051 scopus 로고    scopus 로고
    • Human endothelial nitric oxide synthase: Expression in Escherichia coli, coexpression with calmodulin, and characterization
    • Rodríguez-Crespo, I. and Ortiz de Montellano, P. R. (1996b). Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. Arch. Biochem. Biophys. 336, 151-156.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 151-156
    • Rodríguez-Crespo, I.1    Ortiz de Montellano, P.R.2
  • 39
    • 0040943986 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase: Modulations of the distal heme site produced by progressive N-terminal deletions
    • Rodríguez-Crespo, I., Moenne-Loccoz, P., Loehr, T. M. and Ortiz de Montellano, P. R. (1997). Endothelial nitric oxide synthase: modulations of the distal heme site produced by progressive N-terminal deletions. Biochemistry 36, 8530-8538.
    • (1997) Biochemistry , vol.36 , pp. 8530-8538
    • Rodríguez-Crespo, I.1    Moenne-Loccoz, P.2    Loehr, T.M.3    Ortiz de Montellano, P.R.4
  • 40
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E. and Orci, L. (1992). Molecular dissection of the secretory pathway. Nature 355, 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 41
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J. E. and Linder, M. E. (2004). Palmitoylation of intracellular signaling proteins: regulation and function. Anna. Rev. Biochem. 73, 559-587.
    • (2004) Anna. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 42
    • 84866476582 scopus 로고    scopus 로고
    • Rapid plasma membrane anchoring of newly synthesized p59fyn: Selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3
    • van't Hof, W. and Resh, M. D. (1997). Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3. J. Cell Biol. 136, 1023-1035.
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • van't Hof, W.1    Resh, M.D.2
  • 43
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L. and Casey, P. J. (1996). Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65, 241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


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