메뉴 건너뛰기




Volumn 2, Issue 1, 2011, Pages

Leucine-rich repeat kinase LRRK1 regulates endosomal trafficking of the EGF receptor

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; LEUCINE RICH REPEAT KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 78751627951     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1161     Document Type: Article
Times cited : (73)

References (38)
  • 1
    • 0030036079 scopus 로고    scopus 로고
    • Requirement for the adaptor protein GRB2 in EGF receptor endocytosis
    • Wang, Z. & Moran, M. F. Requirement for the adaptor protein GRB2 in EGF receptor endocytosis. Science 272, 1935-1939 (1996).
    • (1996) Science , vol.272 , pp. 1935-1939
    • Wang, Z.1    Moran, M.F.2
  • 2
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A. V., Lamaze, C. & Schmid, S. L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089 (1996).
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 4
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati, T. & Schliwa, M. Powering membrane traffic in endocytosis and recycling. Nat. Rev. Mol. Cell Biol. 7, 897-908 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 5
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay, D. & Riezman, H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315, 201-205 (2007).
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 6
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., Odorizzi, G. & Emr, S. D. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3, 893-905 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 7
    • 34447109926 scopus 로고    scopus 로고
    • A concentric circle model of multivesicular body cargo sorting
    • Nickerson, D. P., Russell, M. R. & Odorizzi, G. A concentric circle model of multivesicular body cargo sorting. EMBO Rep. 8, 644-650 (2007).
    • (2007) EMBO Rep , vol.8 , pp. 644-650
    • Nickerson, D.P.1    Russell, M.R.2    Odorizzi, G.3
  • 8
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams, R. L. & Urbe, S. The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell Biol. 8, 355-368 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 9
    • 39149132089 scopus 로고    scopus 로고
    • ESCRT complexes and the biogenesis of multivesicular bodies
    • Hurley, J. H. ESCRT complexes and the biogenesis of multivesicular bodies. Curr. Opin. Cell Biol. 20, 4-11 (2008).
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 10
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C. & Stenmark, H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452 (2009).
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 11
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8-linked Parkinsons disease
    • Paisan-Ruiz, C. et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinsons disease. Neuron 44, 595-600 (2004).
    • (2004) Neuron , vol.44 , pp. 595-600
    • Paisan-Ruiz, C.1
  • 12
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • Zimprich, A. et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44, 601-607 (2004).
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1
  • 13
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 14
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson, T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116, 191-203 (2004).
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 15
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • Jiang, X., Huang, F., Marusyk, A. & Sorkin, A. Grb2 regulates internalization of EGF receptors through clathrin-coated pits. Mol. Biol. Cell 14, 858-870 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 16
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • Waterman, H. et al. A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J. 21, 303-313 (2002).
    • (2002) EMBO J , vol.21 , pp. 303-313
    • Waterman, H.1
  • 17
    • 0037106283 scopus 로고    scopus 로고
    • A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics
    • Natsume, T. et al. A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics. Anal. Chem. 74, 4725-4733 (2002).
    • (2002) Anal. Chem , vol.74 , pp. 4725-4733
    • Natsume, T.1
  • 18
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J., Ghigo, E., Kalaidzidis, Y. & Zerial, M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749 (2005).
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 19
    • 33845905221 scopus 로고    scopus 로고
    • Dynein is required for receptor sorting and the morphogenesis of early endosomes
    • Driskell, O. J., Mironov, A., Allan, V. J. & Woodman, P. G. Dynein is required for receptor sorting and the morphogenesis of early endosomes. Nat. Cell Biol. 9, 113-120 (2007).
    • (2007) Nat. Cell Biol , vol.9 , pp. 113-120
    • Driskell, O.J.1    Mironov, A.2    Allan, V.J.3    Woodman, P.G.4
  • 20
    • 47149092772 scopus 로고    scopus 로고
    • Multivesicular bodies: Co-ordinated progression to maturity
    • Woodman, P. G. & Futter, C. E. Multivesicular bodies: co-ordinated progression to maturity. Curr. Opin. Cell Biol. 20, 408-414 (2008).
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 408-414
    • Woodman, P.G.1    Futter, C.E.2
  • 21
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang, L. & Karin, M. Mammalian MAP kinase signalling cascades. Nature 410, 37-40 (2001).
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 23
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinsons disease
    • Ito, G. et al. GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinsons disease. Biochem. 46, 1380-1388 (2007).
    • (2007) Biochem , vol.46 , pp. 1380-1388
    • Ito, G.1
  • 24
    • 48649101425 scopus 로고    scopus 로고
    • ROCO kinase activity is controlled by internal GTPase function
    • Weiss, B. ROCO kinase activity is controlled by internal GTPase function. Sci. Signal. 1, pe27 (2008).
    • (2008) Sci. Signal , vol.1
    • Weiss, B.1
  • 25
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A. & McCormick, F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127 (1991).
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 27
    • 0036094538 scopus 로고    scopus 로고
    • Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
    • Raiborg, C., Bache, K. G., Gillooly, D. J., Madshus, I. H., Stang, E. & Stenmark, H. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nat. Cell Biol. 4, 394-398 (2002).
    • (2002) Nat. Cell Biol , vol.4 , pp. 394-398
    • Raiborg, C.1    Bache, K.G.2    Gillooly, D.J.3    Madshus, I.H.4    Stang, E.5    Stenmark, H.6
  • 28
    • 0242382659 scopus 로고    scopus 로고
    • The UIM domain of Hrs couples receptor sorting to vesicle formation
    • Urbe, S. et al. The UIM domain of Hrs couples receptor sorting to vesicle formation. J. Cell Sci. 116, 4169-4179 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 4169-4179
    • Urbe, S.1
  • 29
    • 33746092492 scopus 로고    scopus 로고
    • Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains
    • Raiborg, C., Wesche, J., Malerod, L. & Stenmark, H. Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J. Cell Sci. 119, 2414-2424 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 2414-2424
    • Raiborg, C.1    Wesche, J.2    Malerod, L.3    Stenmark, H.4
  • 31
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache, K. G., Raiborg, C., Mehlum, A. & Stenmark, H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278, 12513-12521 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 32
    • 33645148675 scopus 로고    scopus 로고
    • Regulation of ubiquitin-binding proteins by monoubiquitination
    • Hoeller, D. et al. Regulation of ubiquitin-binding proteins by monoubiquitination. Nat. Cell Biol. 8, 163-169 (2006).
    • (2006) Nat. Cell Biol , vol.8 , pp. 163-169
    • Hoeller, D.1
  • 33
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451-455 (2002).
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1
  • 34
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento, F., Emans, N., Griffths, G. & Gruenberg, J. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 123, 1373-1387 (1993).
    • (1993) J. Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffths, G.3    Gruenberg, J.4
  • 35
    • 76349109478 scopus 로고    scopus 로고
    • MNUDC is required for plus-end-directed transport of cytoplasmic dynein and dynactins by kinesin-1
    • Yamada, M. et al. mNUDC is required for plus-end-directed transport of cytoplasmic dynein and dynactins by kinesin-1. EMBO J. 29, 517-531 (2010).
    • (2010) EMBO J , vol.29 , pp. 517-531
    • Yamada, M.1
  • 36
    • 69949115962 scopus 로고    scopus 로고
    • CLIP-170-dependent capture of membrane organelles by microtubules initiates minus-end directed transport
    • Lomakin, A. J. et al. CLIP-170-dependent capture of membrane organelles by microtubules initiates minus-end directed transport. Dev. Cell 17, 323-333 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 323-333
    • Lomakin, A.J.1
  • 37
    • 0036847930 scopus 로고    scopus 로고
    • Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway
    • Hanafusa, H., Torii, S., Yasunaga, T. & Nishida, E. Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. Nat. Cell Biol. 4, 850-858 (2002).
    • (2002) Nat. Cell Biol , vol.4 , pp. 850-858
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Nishida, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.