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Volumn 104, Issue 1, 2008, Pages 124-139

Tyr-701 is a new regulatory site for neurotrophin receptor TrkA trafficking and function

Author keywords

Cell differentiation; Degradation; Endocytosis; Kinase activity; Trafficking motif; Tropomyosin related kinase A

Indexed keywords

ASPARTIC ACID; CLATHRIN HEAVY CHAIN; NERVE GROWTH FACTOR; NEUROTROPHIN RECEPTOR; PHENYLALANINE; TROPOMYOSIN RELATED KINASE A RECEPTOR; TYROSINE; UNCLASSIFIED DRUG;

EID: 37249018596     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.05027.x     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 0033971909 scopus 로고    scopus 로고
    • Shp-2 specifically regulates several tyrosine-phosphorylated proteins in brain-derived neurotrophic factor signaling in cultured cerebral cortical neurons
    • Araki T., Yamada M., Ohnishi H., Sano S., Uetsuki T. Hatanaka H. (2000) Shp-2 specifically regulates several tyrosine-phosphorylated proteins in brain-derived neurotrophic factor signaling in cultured cerebral cortical neurons. J. Neurochem. 74, 659 668.
    • (2000) J. Neurochem. , vol.74 , pp. 659-668
    • Araki, T.1    Yamada, M.2    Ohnishi, H.3    Sano, S.4    Uetsuki, T.5    Hatanaka, H.6
  • 2
    • 33646396185 scopus 로고    scopus 로고
    • Cell survival through Trk neurotrophin receptors is differentially regulated by ubiquitination
    • Arevalo J. C., Waite J., Rajagopal R., Beyna M., Chen Z. Y., Lee F. S. Chao M. V. (2006) Cell survival through Trk neurotrophin receptors is differentially regulated by ubiquitination. Neuron 50, 549 559.
    • (2006) Neuron , vol.50 , pp. 549-559
    • Arevalo, J.C.1    Waite, J.2    Rajagopal, R.3    Beyna, M.4    Chen, Z.Y.5    Lee, F.S.6    Chao, M.V.7
  • 5
    • 0034307565 scopus 로고    scopus 로고
    • NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking
    • Beattie E. C., Howe C. L., Wilde A., Brodsky F. M. Mobley W. C. (2000) NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking. J. Neurosci. 20, 7325 7333.
    • (2000) J. Neurosci. , vol.20 , pp. 7325-7333
    • Beattie, E.C.1    Howe, C.L.2    Wilde, A.3    Brodsky, F.M.4    Mobley, W.C.5
  • 6
    • 19744365385 scopus 로고    scopus 로고
    • The single AmphiTrk receptor highlights increased complexity of neurotrophin signalling in vertebrates and suggests an early role in developing sensory neuroepidermal cells
    • Benito-Gutierrez E., Nake C., Llovera M., Comella J. X. Garcia-Fernandez J. (2005) The single AmphiTrk receptor highlights increased complexity of neurotrophin signalling in vertebrates and suggests an early role in developing sensory neuroepidermal cells. Development 132, 2191 2202.
    • (2005) Development , vol.132 , pp. 2191-2202
    • Benito-Gutierrez, E.1    Nake, C.2    Llovera, M.3    Comella, J.X.4    Garcia-Fernandez, J.5
  • 7
    • 0026512998 scopus 로고
    • K-252a inhibits nerve growth factor-induced trk proto-oncogene tyrosine phosphorylation and kinase activity
    • Berg M. M., Sternberg D. W., Parada L. F. Chao M. V. (1992) K-252a inhibits nerve growth factor-induced trk proto-oncogene tyrosine phosphorylation and kinase activity. J. Biol. Chem. 267, 13 16.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13-16
    • Berg, M.M.1    Sternberg, D.W.2    Parada, L.F.3    Chao, M.V.4
  • 8
    • 0032928879 scopus 로고    scopus 로고
    • Caveolin interacts with Trk a and p75(NTR) and regulates neurotrophin signaling pathways
    • Bilderback T. R., Gazula V. R., Lisanti M. P. Dobrowsky R. T. (1999) Caveolin interacts with Trk A and p75(NTR) and regulates neurotrophin signaling pathways. J. Biol. Chem. 274, 257 263.
    • (1999) J. Biol. Chem. , vol.274 , pp. 257-263
    • Bilderback, T.R.1    Gazula, V.R.2    Lisanti, M.P.3    Dobrowsky, R.T.4
  • 9
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J. S. Traub L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395 447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 10
    • 0037547112 scopus 로고    scopus 로고
    • Ligand-induced internalization of the p75 neurotrophin receptor: A slow route to the signaling endosome
    • Bronfman F. C., Tcherpakov M., Jovin T. M. Fainzilber M. (2003) Ligand-induced internalization of the p75 neurotrophin receptor: a slow route to the signaling endosome. J. Neurosci. 23, 3209 3220.
    • (2003) J. Neurosci. , vol.23 , pp. 3209-3220
    • Bronfman, F.C.1    Tcherpakov, M.2    Jovin, T.M.3    Fainzilber, M.4
  • 11
    • 0028076182 scopus 로고
    • An alternatively spliced form of the nerve growth factor receptor TrkA confers an enhanced response to neurotrophin 3
    • Clary D. O. Reichardt L. F. (1994) An alternatively spliced form of the nerve growth factor receptor TrkA confers an enhanced response to neurotrophin 3. Proc. Natl Acad. Sci. USA 91, 11133 11137.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11133-11137
    • Clary, D.O.1    Reichardt, L.F.2
  • 12
    • 0028358645 scopus 로고
    • TrkA cross-linking mimics neuronal responses to nerve growth factor
    • Clary D. O., Weskamp G., Austin L. R. Reichardt L. F. (1994) TrkA cross-linking mimics neuronal responses to nerve growth factor. Mol. Biol. Cell 5, 549 563.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 549-563
    • Clary, D.O.1    Weskamp, G.2    Austin, L.R.3    Reichardt, L.F.4
  • 13
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • Couet J., Sargiacomo M. Lisanti M. P. (1997) Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. J. Biol. Chem. 272, 30429 30438.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 14
    • 0032535448 scopus 로고    scopus 로고
    • A function-structure model for NGF-activated TRK
    • Cunningham M. E. Greene L. A. (1998) A function-structure model for NGF-activated TRK. EMBO J. 17, 7282 7293.
    • (1998) EMBO J. , vol.17 , pp. 7282-7293
    • Cunningham, M.E.1    Greene, L.A.2
  • 15
    • 2442642830 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling
    • Feener E. P., Rosario F., Dunn S. L., Stancheva Z. Myers M. G. Jr. (2004) Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Mol. Cell. Biol. 24, 4968 4978.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4968-4978
    • Feener, E.P.1    Rosario, F.2    Dunn, S.L.3    Stancheva, Z.4    Myers Jr., M.G.5
  • 16
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • Geetha T., Jiang J. Wooten M. W. (2005) Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Mol Cell 20, 301 312.
    • (2005) Mol Cell , vol.20 , pp. 301-312
    • Geetha, T.1    Jiang, J.2    Wooten, M.W.3
  • 17
    • 0030756918 scopus 로고    scopus 로고
    • Transient association of the phosphotyrosine phosphatase SHP-2 with TrkA is induced by nerve growth factor
    • Goldsmith B. A. Koizumi S. (1997) Transient association of the phosphotyrosine phosphatase SHP-2 with TrkA is induced by nerve growth factor. J. Neurochem. 69, 1014 1019.
    • (1997) J. Neurochem. , vol.69 , pp. 1014-1019
    • Goldsmith, B.A.1    Koizumi, S.2
  • 18
    • 0022542457 scopus 로고
    • PC12 cell mutants that possess low- but not high-affinity nerve growth factor receptors neither respond to nor internalize nerve growth factor
    • Green S. H., Rydel R. E., Connolly J. L. Greene L. A. (1986) PC12 cell mutants that possess low- but not high-affinity nerve growth factor receptors neither respond to nor internalize nerve growth factor. J. Cell Biol. 102, 830 843.
    • (1986) J. Cell Biol. , vol.102 , pp. 830-843
    • Green, S.H.1    Rydel, R.E.2    Connolly, J.L.3    Greene, L.A.4
  • 20
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane
    • Harter C. Mellman I. (1992) Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 117, 311 325.
    • (1992) J. Cell Biol. , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 21
    • 0035819073 scopus 로고    scopus 로고
    • NGF signaling from clathrin-coated vesicles: Evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway
    • Howe C. L., Valletta J. S., Rusnak A. S. Mobley W. C. (2001) NGF signaling from clathrin-coated vesicles: evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway. Neuron 32, 801 814.
    • (2001) Neuron , vol.32 , pp. 801-814
    • Howe, C.L.1    Valletta, J.S.2    Rusnak, A.S.3    Mobley, W.C.4
  • 22
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: Roles in neuronal signal transduction
    • Huang E. J. Reichardt L. F. (2003) Trk receptors: roles in neuronal signal transduction. Annu. Rev. Biochem. 72, 609 642.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 23
    • 0037424236 scopus 로고    scopus 로고
    • Trafficking of TrkA-green fluorescent protein chimerae during nerve growth factor-induced differentiation
    • Jullien J., Guili V., Derrington E. A., Darlix J. L., Reichardt L. F. Rudkin B. B. (2003) Trafficking of TrkA-green fluorescent protein chimerae during nerve growth factor-induced differentiation. J. Biol. Chem. 278, 8706 8716.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8706-8716
    • Jullien, J.1    Guili, V.2    Derrington, E.A.3    Darlix, J.L.4    Reichardt, L.F.5    Rudkin, B.B.6
  • 25
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: Analysis by quantitative immunocolocalization
    • Li Q., Lau A., Morris T. J., Guo L., Fordyce C. B. Stanley E. F. (2004) A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J. Neurosci. 24, 4070 4081.
    • (2004) J. Neurosci. , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 26
    • 29244481978 scopus 로고    scopus 로고
    • SLAM-associated protein as a potential negative regulator in Trk signaling
    • Lo K. Y., Chin W. H., Ng Y. P., Cheng A. W., Cheung Z. H. Ip N. Y. (2005) SLAM-associated protein as a potential negative regulator in Trk signaling. J. Biol. Chem. 280, 41744 41752.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41744-41752
    • Lo, K.Y.1    Chin, W.H.2    Ng, Y.P.3    Cheng, A.W.4    Cheung, Z.H.5    Ip, N.Y.6
  • 27
    • 0026091934 scopus 로고
    • The trk proto-oncogene rescues NGF responsiveness in mutant NGF-nonresponsive PC12 cell lines
    • Loeb D. M., Maragos J., Martin-Zanca D., Chao M. V., Parada L. F. Greene L. A. (1991) The trk proto-oncogene rescues NGF responsiveness in mutant NGF-nonresponsive PC12 cell lines. Cell 66, 961 966.
    • (1991) Cell , vol.66 , pp. 961-966
    • Loeb, D.M.1    Maragos, J.2    Martin-Zanca, D.3    Chao, M.V.4    Parada, L.F.5    Greene, L.A.6
  • 28
    • 27344449759 scopus 로고    scopus 로고
    • P75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation
    • Makkerh J. P., Ceni C., Auld D. S., Vaillancourt F., Dorval G. Barker P. A. (2005) p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation. EMBO Rep 6, 936 941.
    • (2005) EMBO Rep , vol.6 , pp. 936-941
    • Makkerh, J.P.1    Ceni, C.2    Auld, D.S.3    Vaillancourt, F.4    Dorval, G.5    Barker, P.A.6
  • 29
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh M. McMahon H. T. (1999) The structural era of endocytosis. Science 285, 215 220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 30
    • 10744230020 scopus 로고    scopus 로고
    • SHP-1 negatively regulates neuronal survival by functioning as a TrkA phosphatase
    • Marsh H. N., Dubreuil C. I., Quevedo C. et al. (2003) SHP-1 negatively regulates neuronal survival by functioning as a TrkA phosphatase. J. Cell Biol. 163, 999 1010.
    • (2003) J. Cell Biol. , vol.163 , pp. 999-1010
    • Marsh, H.N.1    Dubreuil, C.I.2    Quevedo, C.3
  • 32
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; Controlling activity through activation segment conformation
    • Nolen B., Taylor S. Ghosh G. (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15, 661 675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 33
    • 0027374486 scopus 로고
    • Identification of Trk binding sites for SHC and phosphatidylinositol 3′-kinase and formation of a multimeric signaling complex
    • Obermeier A., Lammers R., Wiesmuller K. H., Jung G., Schlessinger J. Ullrich A. (1993) Identification of Trk binding sites for SHC and phosphatidylinositol 3′-kinase and formation of a multimeric signaling complex. J. Biol. Chem. 268, 22963 22966.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22963-22966
    • Obermeier, A.1    Lammers, R.2    Wiesmuller, K.H.3    Jung, G.4    Schlessinger, J.5    Ullrich, A.6
  • 34
    • 0034532063 scopus 로고    scopus 로고
    • PC12 cells have caveolae that contain TrkA. Caveolae-disrupting drugs inhibit nerve growth factor-induced, but not epidermal growth factor-induced, MAPK phosphorylation
    • Peiro S., Comella J. X., Enrich C., Martin-Zanca D. Rocamora N. (2000) PC12 cells have caveolae that contain TrkA. Caveolae-disrupting drugs inhibit nerve growth factor-induced, but not epidermal growth factor-induced, MAPK phosphorylation. J. Biol. Chem. 275, 37846 37852.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37846-37852
    • Peiro, S.1    Comella, J.X.2    Enrich, C.3    Martin-Zanca, D.4    Rocamora, N.5
  • 35
    • 13444292906 scopus 로고    scopus 로고
    • Tyrosine phosphatase SHP-2 is a mediator of activity-dependent neuronal excitotoxicity
    • Rusanescu G., Yang W., Bai A., Neel B. G. Feig L. A. (2005) Tyrosine phosphatase SHP-2 is a mediator of activity-dependent neuronal excitotoxicity. EMBO J. 24, 305 314.
    • (2005) EMBO J. , vol.24 , pp. 305-314
    • Rusanescu, G.1    Yang, W.2    Bai, A.3    Neel, B.G.4    Feig, L.A.5
  • 36
  • 40
    • 33750987920 scopus 로고    scopus 로고
    • Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays
    • Smith M. J., Hardy W. R., Murphy J. M., Jones N. Pawson T. (2006) Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays. Mol. Cell Biol. 26, 8461 8474.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 8461-8474
    • Smith, M.J.1    Hardy, W.R.2    Murphy, J.M.3    Jones, N.4    Pawson, T.5
  • 41
    • 8444221220 scopus 로고    scopus 로고
    • The death receptor antagonist FAIM promotes neurite outgrowth by a mechanism that depends on ERK and NF-kappa B signaling
    • Sole C., Dolcet X., Segura M. F. et al. (2004) The death receptor antagonist FAIM promotes neurite outgrowth by a mechanism that depends on ERK and NF-kappa B signaling. J. Cell Biol. 167, 479 492.
    • (2004) J. Cell Biol. , vol.167 , pp. 479-492
    • Sole, C.1    Dolcet, X.2    Segura, M.F.3
  • 42
    • 0028199799 scopus 로고
    • Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses
    • Stephens R. M., Loeb D. M., Copeland T. D., Pawson T., Greene L. A. Kaplan D. R. (1994) Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses. Neuron 12, 691 705.
    • (1994) Neuron , vol.12 , pp. 691-705
    • Stephens, R.M.1    Loeb, D.M.2    Copeland, T.D.3    Pawson, T.4    Greene, L.A.5    Kaplan, D.R.6
  • 43
    • 0030016334 scopus 로고    scopus 로고
    • A splice variant of the neurotrophin receptor trkB with increased specificity for brain-derived neurotrophic factor
    • Strohmaier C., Carter B. D., Urfer R., Barde Y. A. Dechant G. (1996) A splice variant of the neurotrophin receptor trkB with increased specificity for brain-derived neurotrophic factor. EMBO J. 15, 3332 3337.
    • (1996) EMBO J. , vol.15 , pp. 3332-3337
    • Strohmaier, C.1    Carter, B.D.2    Urfer, R.3    Barde, Y.A.4    Dechant, G.5
  • 44
    • 0036068404 scopus 로고    scopus 로고
    • Shp-2 positively regulates brain-derived neurotrophic factor-promoted survival of cultured ventral mesencephalic dopaminergic neurons through a brain immunoglobulin-like molecule with tyrosine-based activation motifs/Shp substrate-1
    • Takai S., Yamada M., Araki T., Koshimizu H., Nawa H. Hatanaka H. (2002) Shp-2 positively regulates brain-derived neurotrophic factor-promoted survival of cultured ventral mesencephalic dopaminergic neurons through a brain immunoglobulin-like molecule with tyrosine-based activation motifs/Shp substrate-1. J. Neurochem. 82, 353 364.
    • (2002) J. Neurochem. , vol.82 , pp. 353-364
    • Takai, S.1    Yamada, M.2    Araki, T.3    Koshimizu, H.4    Nawa, H.5    Hatanaka, H.6
  • 45
    • 19444366758 scopus 로고    scopus 로고
    • Pincher-mediated macroendocytosis underlies retrograde signaling by neurotrophin receptors
    • Valdez G., Akmentin W., Philippidou P., Kuruvilla R., Ginty D. D. Halegoua S. (2005) Pincher-mediated macroendocytosis underlies retrograde signaling by neurotrophin receptors. J. Neurosci. 25, 5236 5247.
    • (2005) J. Neurosci. , vol.25 , pp. 5236-5247
    • Valdez, G.1    Akmentin, W.2    Philippidou, P.3    Kuruvilla, R.4    Ginty, D.D.5    Halegoua, S.6
  • 46
    • 0025172954 scopus 로고
    • Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail
    • Williams M. A. Fukuda M. (1990) Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell Biol. 111, 955 966.
    • (1990) J. Cell Biol. , vol.111 , pp. 955-966
    • Williams, M.A.1    Fukuda, M.2
  • 47
    • 23044515099 scopus 로고    scopus 로고
    • Functions and mechanisms of retrograde neurotrophin signalling
    • Zweifel L. S., Kuruvilla R. Ginty D. D. (2005) Functions and mechanisms of retrograde neurotrophin signalling. Nat. Rev. Neurosci. 6, 615 625.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 615-625
    • Zweifel, L.S.1    Kuruvilla, R.2    Ginty, D.D.3


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