메뉴 건너뛰기




Volumn 19, Issue 4, 2012, Pages 553-561

Isoform-specific palmitoylation of JNK regulates axonal development

Author keywords

axonal branching; c Jun N terminal kinase JNK; cytoskeleton; isoform regulation; palmitoylation; Wnt pathway

Indexed keywords

STRESS ACTIVATED PROTEIN KINASE;

EID: 84858154205     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2011.124     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 33748942862 scopus 로고    scopus 로고
    • The isoform-specific functions of the c-Jun N-terminal kinases (JNKs): Differences revealed by gene targeting
    • DOI 10.1002/bies.20458
    • Bogoyevitch MA. The isoform-specific functions of the c-Jun N-terminal kinases (JNKs): differences revealed by gene targeting. Bioessays 2006; 28: 923-934. (Pubitemid 44433755)
    • (2006) BioEssays , vol.28 , Issue.9 , pp. 923-934
    • Bogoyevitch, M.A.1
  • 2
    • 79955471332 scopus 로고    scopus 로고
    • The bottleneck of JNK signaling: Molecular and functional characteristics of MKK4 and MKK7
    • Haeusgen W, Herdegen T, Waetzig V. The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7. Eur J Cell Biol 2011; 90: 536-544.
    • (2011) Eur J Cell Biol , vol.90 , pp. 536-544
    • Haeusgen, W.1    Herdegen, T.2    Waetzig, V.3
  • 3
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • DOI 10.1038/39899
    • Yang DD, Kuan CY, Whitmarsh AJ, Rincon M, Zheng TS, Davis RJ et al. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 1997; 389: 865-870. (Pubitemid 27462982)
    • (1997) Nature , vol.389 , Issue.6653 , pp. 865-870
    • Yang, D.D.1    Kuan, C.-Y.2    Whitmarsh, A.J.3    Rincon, M.4    Zheng, T.S.5    Davis, R.J.6    Rakic, P.7    Flavell, R.A.8
  • 7
    • 0346037264 scopus 로고    scopus 로고
    • JNK1 is required for maintenance of neuronal microtubules and controls phosphorylation of microtubule-associated proteins
    • DOI 10.1016/S1534-5807(03)00094-7, PII S1534580703000947
    • Chang L, Jones Y, Ellisman MH, Goldstein LS, Karin M. JNK1 is required for maintenance of neuronal microtubules and controls phosphorylation of microtubule-associated proteins. Dev Cell 2003; 4: 521-533. (Pubitemid 36437559)
    • (2003) Developmental Cell , vol.4 , Issue.4 , pp. 521-533
    • Chang, L.1    Jones, Y.2    Ellisman, M.H.3    Goldstein, L.S.B.4    Karin, M.5
  • 8
    • 33646095177 scopus 로고    scopus 로고
    • JNK1 phosphorylation of SCG10 determines microtubule dynamics and axodendritic length
    • Tararuk T, Ostman N, Li W, Bjorkblom B, Padzik A, Zdrojewska J et al. JNK1 phosphorylation of SCG10 determines microtubule dynamics and axodendritic length. J Cell Biol 2006; 173: 265-277.
    • (2006) J Cell Biol , vol.173 , pp. 265-277
    • Tararuk, T.1    Ostman, N.2    Li, W.3    Bjorkblom, B.4    Padzik, A.5    Zdrojewska, J.6
  • 9
    • 21844475890 scopus 로고    scopus 로고
    • Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: Role of microtubule-associated protein 2 as an effector
    • DOI 10.1523/JNEUROSCI.1517-05.2005
    • Bjorkblom B, Ostman N, Hongisto V, Komarovski V, Filen JJ, Nyman TA et al. Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: role of microtubule-associated protein 2 as an effector. J Neurosci 2005; 25: 6350-6361. (Pubitemid 40962530)
    • (2005) Journal of Neuroscience , vol.25 , Issue.27 , pp. 6350-6361
    • Bjorkblom, B.1    Ostman, N.2    Hongisto, V.3    Komarovski, V.4    Filen, J.-J.5    Nyman, T.A.6    Kallunki, T.7    Courtney, M.J.8    Coffey, E.T.9
  • 10
    • 0037414797 scopus 로고    scopus 로고
    • A single c-Jun N-terminal kinase isoform (JNK3-p54) is an effector in both neuronal differentiation and cell death
    • DOI 10.1074/jbc.M207391200
    • Waetzig V, Herdegen T. A single c-Jun N-terminal kinase isoform (JNK3-p54) is an effector in both neuronal differentiation and cell death. J Biol Chem 2003; 278: 567-572. (Pubitemid 36043610)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 567-572
    • Waetzig, V.1    Herdegen, T.2
  • 11
    • 34547737016 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK) cooperates with Gsk3beta to regulate Dishevelled-mediated microtubule stability
    • Ciani L, Salinas PC. c-Jun N-terminal kinase (JNK) cooperates with Gsk3beta to regulate Dishevelled-mediated microtubule stability. BMC Cell Biol 2007; 8: 27.
    • (2007) BMC Cell Biol , vol.8 , pp. 27
    • Ciani, L.1    Salinas, P.C.2
  • 12
    • 20444403334 scopus 로고    scopus 로고
    • Physiological regulation of the β-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation
    • DOI 10.1523/JNEUROSCI.4883-04.2005
    • Kimberly WT, Zheng JB, Town T, Flavell RA, Selkoe DJ. Physiological regulation of the beta-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation. J Neurosci 2005; 25: 5533-5543. (Pubitemid 40800645)
    • (2005) Journal of Neuroscience , vol.25 , Issue.23 , pp. 5533-5543
    • Taylor Kimberly, W.1    Zheng, J.B.2    Town, T.3    Flavell, R.A.4    Selkoe, D.J.5
  • 13
    • 33748689930 scopus 로고    scopus 로고
    • Activated c-Jun N-terminal kinase is required for axon formation
    • DOI 10.1523/JNEUROSCI.2625-06.2006
    • Oliva Jr AA, Atkins CM, Copenagle L, Banker GA. Activated c-Jun N-terminal kinase is required for axon formation. J Neurosci 2006; 26: 9462-9470. (Pubitemid 44396859)
    • (2006) Journal of Neuroscience , vol.26 , Issue.37 , pp. 9462-9470
    • Oliva Jr., A.A.1    Atkins, C.M.2    Copenagle, L.3    Banker, G.A.4
  • 14
    • 16644381829 scopus 로고    scopus 로고
    • Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development
    • DOI 10.1038/nn1374
    • Rosso SB, Sussman D, Wynshaw-Boris A, Salinas PC. Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development. Nat Neurosci 2005; 8: 34-42. (Pubitemid 41236729)
    • (2005) Nature Neuroscience , vol.8 , Issue.1 , pp. 34-42
    • Rosso, S.B.1    Sussman, D.2    Wynshaw-Boris, A.3    Salinas, P.C.4
  • 15
    • 0031469645 scopus 로고    scopus 로고
    • WNT-7a induces axonal remodeling and increases synapsin I levels in cerebellar neurons
    • DOI 10.1006/dbio.1997.8734
    • Lucas FR, Salinas PC. WNT-7a induces axonal remodeling and increases synapsin I levels in cerebellar neurons. Dev Biol 1997; 192: 31-44. (Pubitemid 28015644)
    • (1997) Developmental Biology , vol.192 , Issue.1 , pp. 31-44
    • Lucas, F.R.1    Salinas, P.C.2
  • 16
    • 48249110960 scopus 로고    scopus 로고
    • Wnt signaling in neural circuit assembly
    • Salinas PC, Zou Y. Wnt signaling in neural circuit assembly. Annu Rev Neurosci 2008; 31: 339-358.
    • (2008) Annu Rev Neurosci , vol.31 , pp. 339-358
    • Salinas, P.C.1    Zou, Y.2
  • 17
    • 33845653234 scopus 로고    scopus 로고
    • Uses for JNK: The many and varied substrates of the c-Jun N-terminal kinases
    • DOI 10.1128/MMBR.00025-06
    • Bogoyevitch MA, Kobe B. Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases. Microbiol Mol Biol Rev 2006; 70: 1061-1095. (Pubitemid 44958264)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.4 , pp. 1061-1095
    • Bogoyevitch, M.A.1    Kobe, B.2
  • 18
    • 0033118607 scopus 로고    scopus 로고
    • The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development
    • DOI 10.1016/S0896-6273(00)80727-8
    • Kuan CY, Yang DD, Samanta Roy DR, Davis RJ, Rakic P, Flavell RA. The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 1999; 22: 667-676. (Pubitemid 29203491)
    • (1999) Neuron , vol.22 , Issue.4 , pp. 667-676
    • Kuan, C.-Y.1    Yang, D.D.2    Samanta Roy, D.R.3    Davis, R.J.4    Rakic, P.5    Flavell, R.A.6
  • 20
    • 0036779578 scopus 로고    scopus 로고
    • Protein palmitoylation: A regulator of neuronal development and function
    • DOI 10.1038/nrn940
    • El-Husseini Ael D, Bredt DS. Protein palmitoylation: a regulator of neuronal development and function. Nat Rev Neurosci 2002; 3: 791-802. (Pubitemid 135706690)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.10 , pp. 791-802
    • El-Husseini, A.E.-D.1    Bredt, D.S.2
  • 21
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • DOI 10.1016/S0962-8924(02)00008-9, PII S0962892402000089
    • Bijlmakers MJ, Marsh M. The on-off story of protein palmitoylation. Trends Cell Biol 2003; 13: 32-42. (Pubitemid 35453893)
    • (2003) Trends in Cell Biology , vol.13 , Issue.1 , pp. 32-42
    • Bijlmakers, M.-J.1    Marsh, M.2
  • 22
    • 67649867067 scopus 로고    scopus 로고
    • Subunit-selective palmitoylation regulates the intracellular trafficking of AMPA receptor
    • Yang G, Xiong W, Kojic L, Cynader MS. Subunit-selective palmitoylation regulates the intracellular trafficking of AMPA receptor. Eur J Neurosci 2009; 30: 35-46.
    • (2009) Eur J Neurosci , vol.30 , pp. 35-46
    • Yang, G.1    Xiong, W.2    Kojic, L.3    Cynader, M.S.4
  • 23
    • 0035907126 scopus 로고    scopus 로고
    • Differential palmitoylation of two mouse glutamate receptor interacting protein 1 forms with different N-terminal sequences
    • DOI 10.1016/S0304-3940(01)01766-9, PII S0304394001017669
    • Yamazaki M, Fukaya M, Abe M, Ikeno K, Kakizaki T, Watanabe M et al. Differential palmitoylation of two mouse glutamate receptor interacting protein 1 forms with different N-terminal sequences. Neurosci Lett 2001; 304: 81-84. (Pubitemid 32373321)
    • (2001) Neuroscience Letters , vol.304 , Issue.1-2 , pp. 81-84
    • Yamazaki, M.1    Fukaya, M.2    Abe, M.3    Ikeno, K.4    Kakizaki, T.5    Watanabe, M.6    Sakimura, K.7
  • 24
    • 47049121578 scopus 로고    scopus 로고
    • The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus
    • Guo C, Whitmarsh AJ. The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus. J Biol Chem 2008; 283: 15903-15911.
    • (2008) J Biol Chem , vol.283 , pp. 15903-15911
    • Guo, C.1    Whitmarsh, A.J.2
  • 25
    • 67049162113 scopus 로고    scopus 로고
    • Wnt5a mediates nerve growth factor-dependent axonal branching and growth in developing sympathetic neurons
    • Bodmer D, Levine-Wilkinson S, Richmond A, Hirsh S, Kuruvilla R. Wnt5a mediates nerve growth factor-dependent axonal branching and growth in developing sympathetic neurons. J Neurosci 2009; 29: 7569-7581.
    • (2009) J Neurosci , vol.29 , pp. 7569-7581
    • Bodmer, D.1    Levine-Wilkinson, S.2    Richmond, A.3    Hirsh, S.4    Kuruvilla, R.5
  • 26
    • 0034934782 scopus 로고    scopus 로고
    • Glutamate regulates actin-based motility in axonal filopodia
    • DOI 10.1038/90489
    • Chang S, De Camilli P. Glutamate regulates actin-based motility in axonal filopodia. Nat Neurosci 2001; 4: 787-793. (Pubitemid 32702510)
    • (2001) Nature Neuroscience , vol.4 , Issue.8 , pp. 787-793
    • Chang, S.1    De Camilli, P.2
  • 27
    • 40749130495 scopus 로고    scopus 로고
    • Proapoptotic role of Hsp90 by its interaction with c-Jun N-terminal kinase in lipid rafts in edelfosine-mediated antileukemic therapy
    • DOI 10.1038/sj.onc.1210816, PII 1210816
    • Nieto-Miguel T, Gajate C, Gonzalez-Camacho F, Mollinedo F. Proapoptotic role of Hsp90 by its interaction with c-Jun N-terminal kinase in lipid rafts in edelfosine-mediated antileukemic therapy. Oncogene 2008; 27: 1779-1787. (Pubitemid 351380270)
    • (2008) Oncogene , vol.27 , Issue.12 , pp. 1779-1787
    • Nieto-Miguel, T.1    Gajate, C.2    Gonzalez-Camacho, F.3    Mollinedo, F.4
  • 29
    • 14944344230 scopus 로고    scopus 로고
    • Integrin-dependent interaction of lipid rafts with the actin cytoskeleton in activated human platelets
    • DOI 10.1242/jcs.01648
    • Bodin S, Soulet C, Tronchere H, Sie P, Gachet C, Plantavid M et al. Integrin-dependent interaction of lipid rafts with the actin cytoskeleton in activated human platelets. J Cell Sci 2005; 118 (Pt 4): 759-769. (Pubitemid 40372584)
    • (2005) Journal of Cell Science , vol.118 , Issue.4 , pp. 759-769
    • Bodin, S.1    Soulet, C.2    Tronchere, H.3    Sie, P.4    Gachet, C.5    Plantavid, M.6    Payrastre, B.7
  • 30
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • DOI 10.1146/annurev.cellbio.18.031802.150501
    • Luo L. Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu Rev Cell Dev Biol 2002; 18: 601-635. (Pubitemid 35387363)
    • (2002) Annual Review of Cell and Developmental Biology , vol.18 , pp. 601-635
    • Luo, L.1
  • 31
    • 65649086782 scopus 로고    scopus 로고
    • Wnt signaling mediates experience-related regulation of synapse numbers and mossy fiber connectivities in the adult hippocampus
    • Gogolla N, Galimberti I, Deguchi Y, Caroni P. Wnt signaling mediates experience-related regulation of synapse numbers and mossy fiber connectivities in the adult hippocampus. Neuron 2009; 62: 510-525.
    • (2009) Neuron , vol.62 , pp. 510-525
    • Gogolla, N.1    Galimberti, I.2    Deguchi, Y.3    Caroni, P.4
  • 32
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel RC, Green WN. Labeling and quantifying sites of protein palmitoylation. Biotechniques 2004; 36: 276-285. (Pubitemid 38174735)
    • (2004) BioTechniques , vol.36 , Issue.2 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 33
    • 57249086469 scopus 로고    scopus 로고
    • Wnts acting through canonical and noncanonical signaling pathways exert opposite effects on hippocampal synapse formation
    • Davis EK, Zou Y, Ghosh A. Wnts acting through canonical and noncanonical signaling pathways exert opposite effects on hippocampal synapse formation. Neural Dev 2008; 3: 32.
    • (2008) Neural Dev , vol.3 , pp. 32
    • Davis, E.K.1    Zou, Y.2    Ghosh, A.3
  • 35
    • 0032476649 scopus 로고    scopus 로고
    • Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons and implicated in plasma membrane dynamics and cell process formation
    • DOI 10.1083/jcb.143.3.795
    • Kutzleb C, Sanders G, Yamamoto R, Wang X, Lichte B, Petrasch-Parwez E et al. Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons and implicated in plasma membrane dynamics and cell process formation. J Cell Biol 1998; 143: 795-813. (Pubitemid 28512572)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 795-813
    • Kutzleb, C.1    Sanders, G.2    Yamamoto, R.3    Wang, X.4    Lichte, B.5    Petrasch-Parwez, E.6    Kilimann, M.W.7
  • 36
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • El-Husseini AE, Craven SE, Chetkovich DM, Firestein BL, Schnell E, Aoki C et al. Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J Cell Biol 2000; 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
  • 38
    • 67349094513 scopus 로고    scopus 로고
    • Cerebral ischemia provokes a profound exchange of activated JNK isoforms in brain mitochondria
    • Zhao Y, Herdegen T. Cerebral ischemia provokes a profound exchange of activated JNK isoforms in brain mitochondria. Mol Cell Neurosci 2009; 41: 186-195.
    • (2009) Mol Cell Neurosci , vol.41 , pp. 186-195
    • Zhao, Y.1    Herdegen, T.2
  • 39
    • 28544435630 scopus 로고    scopus 로고
    • Inhibited neurogenesis in JNK1-deficient embryonic stem cells
    • DOI 10.1128/MCB.25.24.10791-10802.2005
    • Amura CR, Marek L, Winn RA, Heasley LE. Inhibited neurogenesis in JNK1-deficient embryonic stem cells. Mol Cell Biol 2005; 25: 10791-10802. (Pubitemid 41747124)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.24 , pp. 10791-10802
    • Amura, C.R.1    Marek, L.2    Winn, R.A.3    Heasley, L.E.4
  • 40
    • 0038495741 scopus 로고    scopus 로고
    • JNK phosphorylates paxillin and regulates cell migration
    • DOI 10.1038/nature01745
    • Huang C, Rajfur Z, Borchers C, Schaller MD, Jacobson K. JNK phosphorylates paxillin and regulates cell migration. Nature 2003; 424: 219-223. (Pubitemid 36858692)
    • (2003) Nature , vol.424 , Issue.6945 , pp. 219-223
    • Huang, C.1    Rajfur, Z.2    Borchers, C.3    Schaller, M.D.4    Jacobson, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.