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Volumn 6, Issue , 2015, Pages

LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; COFILIN; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 7; EPIDERMAL GROWTH FACTOR RECEPTOR; F ACTIN; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE 2; GLYCOGEN SYNTHASE KINASE 3BETA; LEUCINE RICH REPEAT KINASE 2; P21 ACTIVATED KINASE 1; PLATELET DERIVED GROWTH FACTOR RECEPTOR; SOMATOMEDIN C RECEPTOR; URIDINE DIPHOSPHATE; VASODILATOR STIMULATED PHOSPHOPROTEIN; LRRK2 PROTEIN, HUMAN; LRRK2 PROTEIN, MOUSE; LRRK2 PROTEIN, RAT; PROTEIN SERINE THREONINE KINASE;

EID: 84941635707     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9255     Document Type: Review
Times cited : (81)

References (71)
  • 2
    • 79955544006 scopus 로고    scopus 로고
    • Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)
    • Chan, D., Citro, A., Cordy, J. M., Shen, G. C. & Wolozin, B. Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2). J. Biol. Chem. 286, 16140-16149 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 16140-16149
    • Chan, D.1    Citro, A.2    Cordy, J.M.3    Shen, G.C.4    Wolozin, B.5
  • 3
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: Characterization of how Parkinsons disease mutants affect kinase activity
    • Jaleel, M. et al. LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinsons disease mutants affect kinase activity. Biochem. J. 405, 307-317 (2007).
    • (2007) Biochem. J. , vol.405 , pp. 307-317
    • Jaleel, M.1
  • 4
    • 70449377127 scopus 로고    scopus 로고
    • Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis
    • Parisiadou, L. et al. Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis. J. Neurosci. 29, 13971-13980 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 13971-13980
    • Parisiadou, L.1
  • 5
    • 77957929468 scopus 로고    scopus 로고
    • A QUICK screen for Lrrk2 interaction partners-leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics
    • Meixner, A. et al. A QUICK screen for Lrrk2 interaction partners-leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol. Cell. Proteomics 10, 001172 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 001172
    • Meixner, A.1
  • 6
  • 7
    • 31344432937 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinsons disease in North African Arabs
    • Lesage, S. et al. LRRK2 G2019S as a cause of Parkinsons disease in North African Arabs. N. Engl. J. Med. 354, 422-423 (2006).
    • (2006) N. Engl. J. Med. , vol.354 , pp. 422-423
    • Lesage, S.1
  • 8
    • 31344439221 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinsons disease in Ashkenazi Jews
    • Ozelius, L. J. et al. LRRK2 G2019S as a cause of Parkinsons disease in Ashkenazi Jews. N. Engl. J. Med. 354, 424-425 (2006).
    • (2006) N. Engl. J. Med. , vol.354 , pp. 424-425
    • Ozelius, L.J.1
  • 9
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • Smith, W. W. et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc. Natl Acad. Sci. USA 102, 18676-18681 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18676-18681
    • Smith, W.W.1
  • 10
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod, D. et al. The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 52, 587-593 (2006).
    • (2006) Neuron , vol.52 , pp. 587-593
    • MacLeod, D.1
  • 11
    • 84862703407 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) as a potential therapeutic target in Parkinsons disease
    • Lee, B. D., Dawson, V. L. & Dawson, T. M. Leucine-rich repeat kinase 2 (LRRK2) as a potential therapeutic target in Parkinsons disease. Trends Pharmacol. Sci. 33, 365-373 (2012).
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 365-373
    • Lee, B.D.1    Dawson, V.L.2    Dawson, T.M.3
  • 12
    • 19744380563 scopus 로고    scopus 로고
    • Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
    • Nimmerjahn, A., Kirchhoff, F. & Helmchen, F. Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo. Science 308, 1314-1318 (2005).
    • (2005) Science , vol.308 , pp. 1314-1318
    • Nimmerjahn, A.1    Kirchhoff, F.2    Helmchen, F.3
  • 13
    • 22244464662 scopus 로고    scopus 로고
    • ATP mediates rapid microglial response to local brain injury in vivo
    • Davalos, D. et al. ATP mediates rapid microglial response to local brain injury in vivo. Nat. Neurosci. 8, 752-758 (2005).
    • (2005) Nat. Neurosci. , vol.8 , pp. 752-758
    • Davalos, D.1
  • 14
    • 84870832562 scopus 로고    scopus 로고
    • Reciprocal regulation between resting microglial dynamics and neuronal activity in vivo
    • Li, Y., Du, X. F., Liu, C. S., Wen, Z. L. & Du, J. L. Reciprocal regulation between resting microglial dynamics and neuronal activity in vivo. Dev. Cell 23, 1189-1202 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 1189-1202
    • Li, Y.1    Du, X.F.2    Liu, C.S.3    Wen, Z.L.4    Du, J.L.5
  • 15
    • 70449650338 scopus 로고    scopus 로고
    • Microglia processes block the spread of damage in the brain and require functional chloride channels
    • Hines, D. J., Hines, R. M., Mulligan, S. J. & Macvicar, B. A. Microglia processes block the spread of damage in the brain and require functional chloride channels. Glia 57, 1610-1618 (2009).
    • (2009) Glia , vol.57 , pp. 1610-1618
    • Hines, D.J.1    Hines, R.M.2    Mulligan, S.J.3    Macvicar, B.A.4
  • 16
    • 78149456920 scopus 로고    scopus 로고
    • Inflammatory responses are not sufficient to cause delayed neuronal death in ATP-induced acute brain injury
    • Jeong, H. K. et al. Inflammatory responses are not sufficient to cause delayed neuronal death in ATP-induced acute brain injury. PLoS One 5, e13756 (2010).
    • (2010) PLoS One , vol.5 , pp. e13756
    • Jeong, H.K.1
  • 17
    • 84883612112 scopus 로고    scopus 로고
    • Brain inflammation and microglia: Facts and misconceptions
    • Jeong, H. K., Ji, K., Min, K. & Joe, E. H. Brain inflammation and microglia: facts and misconceptions. Exp. Neurobiol. 22, 59-67 (2013).
    • (2013) Exp. Neurobiol. , vol.22 , pp. 59-67
    • Jeong, H.K.1    Ji, K.2    Min, K.3    Joe, E.H.4
  • 18
    • 34147115541 scopus 로고    scopus 로고
    • Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
    • El Khoury, J. et al. Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease. Nat. Med. 13, 432-438 (2007).
    • (2007) Nat. Med. , vol.13 , pp. 432-438
    • El Khoury, J.1
  • 19
    • 84870534288 scopus 로고    scopus 로고
    • Mutant huntingtin impairs immune cell migration in Huntington disease
    • Kwan, W. et al. Mutant huntingtin impairs immune cell migration in Huntington disease. J. Clin. Invest. 122, 4737-4747 (2012).
    • (2012) J. Clin. Invest. , vol.122 , pp. 4737-4747
    • Kwan, W.1
  • 20
    • 79952610280 scopus 로고    scopus 로고
    • Age-related alterations in the dynamic behavior of microglia
    • Damani, M. R. et al. Age-related alterations in the dynamic behavior of microglia. Aging Cell 10, 263-276 (2011).
    • (2011) Aging Cell , vol.10 , pp. 263-276
    • Damani, M.R.1
  • 21
    • 84892514122 scopus 로고    scopus 로고
    • Homeostatic and injury-induced microglia behavior in the aging brain
    • Hefendehl, J. K. et al. Homeostatic and injury-induced microglia behavior in the aging brain. Aging Cell 13, 60-69 (2014).
    • (2014) Aging Cell , vol.13 , pp. 60-69
    • Hefendehl, J.K.1
  • 22
    • 84859499649 scopus 로고    scopus 로고
    • Impaired inflammatory responses in murine Lrrk2-knockdown brain microglia
    • Kim, B. et al. Impaired inflammatory responses in murine Lrrk2-knockdown brain microglia. PLoS One 7, e34693 (2012).
    • (2012) PLoS One , vol.7 , pp. e34693
    • Kim, B.1
  • 23
    • 84856632181 scopus 로고    scopus 로고
    • LRRK2 inhibition attenuates microglial inflammatory responses
    • Moehle, M. S. et al. LRRK2 inhibition attenuates microglial inflammatory responses. J. Neurosci. 32, 1602-1611 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 1602-1611
    • Moehle, M.S.1
  • 24
    • 38149070791 scopus 로고    scopus 로고
    • Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation
    • Lim, S. T. et al. Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation. Mol. Cell 29, 9-22 (2008).
    • (2008) Mol. Cell , vol.29 , pp. 9-22
    • Lim, S.T.1
  • 25
    • 0037409464 scopus 로고    scopus 로고
    • FAK overexpression upregulates cyclin D3 and enhances cell proliferation via the PKC and PI3-kinase-Akt pathways
    • Yamamoto, D. et al. FAK overexpression upregulates cyclin D3 and enhances cell proliferation via the PKC and PI3-kinase-Akt pathways. Cell. Signal. 15, 575-583 (2003).
    • (2003) Cell. Signal. , vol.15 , pp. 575-583
    • Yamamoto, D.1
  • 26
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • Mitra, S. K., Hanson, D. A. & Schlaepfer, D. D. Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 27
    • 2942596543 scopus 로고    scopus 로고
    • FERM domain interaction promotes FAK signaling
    • Dunty, J. M. et al. FERM domain interaction promotes FAK signaling. Mol. Cell. Biol. 24, 5353-5368 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5353-5368
    • Dunty, J.M.1
  • 28
    • 0031917388 scopus 로고    scopus 로고
    • Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion
    • Zheng, C. et al. Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion. J. Biol. Chem. 273, 2384-2389 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2384-2389
    • Zheng, C.1
  • 29
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins
    • Kornberg, L. J., Earp, H. S., Turner, C. E., Prockop, C. & Juliano, R. L. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins. Proc. Natl Acad. Sci. USA 88, 8392-8396 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 30
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan, J. L., Trevithick, J. E. & Hynes, R. O. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell. Regul. 2, 951-964 (1991).
    • (1991) Cell. Regul. , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 31
    • 0030760119 scopus 로고    scopus 로고
    • Role of integrins in cellular responses to mechanical stress and adhesion
    • Shyy, J. Y. & Chien, S. Role of integrins in cellular responses to mechanical stress and adhesion. Curr. Opin. Cell Biol. 9, 707-713 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 707-713
    • Shyy, J.Y.1    Chien, S.2
  • 32
    • 0032938716 scopus 로고    scopus 로고
    • Regulation of tyrosine kinase cascades by G-protein-coupled receptors
    • Luttrell, L. M., Daaka, Y. & Lefkowitz, R. J. Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177-183 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 177-183
    • Luttrell, L.M.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 33
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg, D. J. et al. FAK integrates growth-factor and integrin signals to promote cell migration. Nat. Cell Biol. 2, 249-256 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 249-256
    • Sieg, D.J.1
  • 34
    • 35848943698 scopus 로고    scopus 로고
    • Mitogenic signaling pathways induced by G protein-coupled receptors
    • Rozengurt, E. Mitogenic signaling pathways induced by G protein-coupled receptors. J. Cell Physiol. 213, 589-602 (2007).
    • (2007) J. Cell Physiol. , vol.213 , pp. 589-602
    • Rozengurt, E.1
  • 35
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement
    • Parsons, J. T., Martin, K. H., Slack, J. K., Taylor, J. M. & Weed, S. A. Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene 19, 5606-5613 (2000).
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 36
    • 33845259342 scopus 로고    scopus 로고
    • The P2Y12 receptor regulates microglial activation by extracellular nucleotides
    • Haynes, S. E. et al. The P2Y12 receptor regulates microglial activation by extracellular nucleotides. Nat. Neurosci. 9, 1512-1519 (2006).
    • (2006) Nat. Neurosci. , vol.9 , pp. 1512-1519
    • Haynes, S.E.1
  • 37
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller, M. D. et al. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell Biol. 14, 1680-1688 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1
  • 38
    • 34447538483 scopus 로고    scopus 로고
    • Cellular characterization of a novel focal adhesion kinase inhibitor
    • Slack-Davis, J. K. et al. Cellular characterization of a novel focal adhesion kinase inhibitor. J. Biol. Chem. 282, 14845-14852 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14845-14852
    • Slack-Davis, J.K.1
  • 39
    • 57349153946 scopus 로고    scopus 로고
    • A small molecule inhibitor 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth
    • Golubovskaya, V. M. et al. A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth. J. Med. Chem. 51, 7405-7416 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 7405-7416
    • Golubovskaya, V.M.1
  • 40
    • 84876720453 scopus 로고    scopus 로고
    • Mitoxantrone targets the ATP-binding site of FAK, binds the FAK kinase domain and decreases FAK, Pyk-2, c-Src, and IGF-1R in vitro kinase activities
    • Golubovskaya, V. M. et al. Mitoxantrone targets the ATP-binding site of FAK, binds the FAK kinase domain and decreases FAK, Pyk-2, c-Src, and IGF-1R in vitro kinase activities. Anticancer Agents Med. Chem. 13, 546-554 (2013).
    • (2013) Anticancer Agents Med. Chem. , vol.13 , pp. 546-554
    • Golubovskaya, V.M.1
  • 41
    • 78149435654 scopus 로고    scopus 로고
    • Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif
    • Pungaliya, P. P. et al. Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif. PLoS ONE 5, e13672 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e13672
    • Pungaliya, P.P.1
  • 42
    • 70350653779 scopus 로고    scopus 로고
    • Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinsons disease
    • Nichols, R. J. et al. Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinsons disease. Biochem. J. 424, 47-60 (2009).
    • (2009) Biochem. J. , vol.424 , pp. 47-60
    • Nichols, R.J.1
  • 43
    • 84879024830 scopus 로고    scopus 로고
    • Comprehensive characterization and optimization of anti- LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies
    • Davies, P. et al. Comprehensive characterization and optimization of anti- LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies. Biochem. J. 453, 101-113 (2013).
    • (2013) Biochem. J. , vol.453 , pp. 101-113
    • Davies, P.1
  • 44
    • 84865149238 scopus 로고    scopus 로고
    • GSK2578215A; A potent and highly selective 2- arylmethyloxy-5-substitutent-N-arylbenzamide LRRK2 kinase inhibitor
    • Reith, A. D. et al. GSK2578215A; a potent and highly selective 2- arylmethyloxy-5-substitutent-N-arylbenzamide LRRK2 kinase inhibitor. Bioorg. Med. Chem. Lett. 22, 5625-5629 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 5625-5629
    • Reith, A.D.1
  • 45
    • 79952918505 scopus 로고    scopus 로고
    • Characterization of a selective inhibitor of the Parkinsons disease kinase LRRK2
    • Deng, X. et al. Characterization of a selective inhibitor of the Parkinsons disease kinase LRRK2. Nat. Chem. Biol. 7, 203-205 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 203-205
    • Deng, X.1
  • 46
    • 80054977424 scopus 로고    scopus 로고
    • Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinsons disease-related toxicity in human neurons
    • Ramsden, N. et al. Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinsons disease-related toxicity in human neurons. ACS Chem. Biol. 6, 1021-1028 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1021-1028
    • Ramsden, N.1
  • 47
    • 77956441086 scopus 로고    scopus 로고
    • Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinsons disease
    • Lee, B. D. et al. Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinsons disease. Nat. Med. 16, 998-1000 (2010).
    • (2010) Nat. Med. , vol.16 , pp. 998-1000
    • Lee, B.D.1
  • 48
    • 0033179479 scopus 로고    scopus 로고
    • Paradoxical activation of Raf by a novel Raf inhibitor
    • Hall-Jackson, C. A. et al. Paradoxical activation of Raf by a novel Raf inhibitor. Chem. Biol. 6, 559-568 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 559-568
    • Hall-Jackson, C.A.1
  • 49
    • 15444376695 scopus 로고    scopus 로고
    • Raf-1 regulates Rho signaling and cell migration
    • Ehrenreiter, K. et al. Raf-1 regulates Rho signaling and cell migration. J. Cell Biol. 168, 955-964 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 955-964
    • Ehrenreiter, K.1
  • 50
    • 85018214550 scopus 로고    scopus 로고
    • The G2019S LRRK2 mutation increases myeloid cell chemotactic responses and enhances LRRK2 binding to actin-regulatory proteins
    • Moehle, M. S. et al. The G2019S LRRK2 mutation increases myeloid cell chemotactic responses and enhances LRRK2 binding to actin-regulatory proteins. Hum. Mol. Genet. 24, 4250-4267 (2015).
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 4250-4267
    • Moehle, M.S.1
  • 51
    • 84876318823 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 functionally interacts with microtubules and kinase-dependently modulates cell migration
    • Caesar, M. et al. Leucine-rich repeat kinase 2 functionally interacts with microtubules and kinase-dependently modulates cell migration. Neurobiol. Dis. 54, 280-288 (2013).
    • (2013) Neurobiol. Dis. , vol.54 , pp. 280-288
    • Caesar, M.1
  • 52
    • 3142763039 scopus 로고    scopus 로고
    • Actin and microtubules in cell motility: Which one is in control?
    • Etienne-Manneville, S. Actin and microtubules in cell motility: which one is in control? Traffic 5, 470-477 (2004).
    • (2004) Traffic , vol.5 , pp. 470-477
    • Etienne-Manneville, S.1
  • 53
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic, D. et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377, 539-544 (1995).
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1
  • 54
    • 0037057293 scopus 로고    scopus 로고
    • Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397
    • Leu, T. H. & Maa, M. C. Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397. Oncogene 21, 6992-7000 (2002).
    • (2002) Oncogene , vol.21 , pp. 6992-7000
    • Leu, T.H.1    Maa, M.C.2
  • 55
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb, M. B., Polte, T. R. & Hanks, S. K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 15, 954-963 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 56
    • 79953309890 scopus 로고    scopus 로고
    • FAK phosphorylation at Tyr-925 regulates cross-talk between focal adhesion turnover and cell protrusion
    • Deramaudt, T. B. et al. FAK phosphorylation at Tyr-925 regulates cross-talk between focal adhesion turnover and cell protrusion. Mol. Biol. Cell 22, 964-975 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 964-975
    • Deramaudt, T.B.1
  • 57
    • 0030597218 scopus 로고    scopus 로고
    • Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src
    • Calalb, M. B., Zhang, X., Polte, T. R. & Hanks, S. K. Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src. Biochem. Biophys. Res. Commun. 228, 662-668 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 662-668
    • Calalb, M.B.1    Zhang, X.2    Polte, T.R.3    Hanks, S.K.4
  • 58
    • 21644483424 scopus 로고    scopus 로고
    • Focal adhesion kinase is required for the spatial organization of the leading edge in migrating cells
    • Tilghman, R. W. et al. Focal adhesion kinase is required for the spatial organization of the leading edge in migrating cells. J. Cell Sci. 118, 2613-2623 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 2613-2623
    • Tilghman, R.W.1
  • 59
    • 0042329506 scopus 로고    scopus 로고
    • Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration
    • Xie, Z., Sanada, K., Samuels, B. A., Shih, H. & Tsai, L. H. Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration. Cell 114, 469-482 (2003).
    • (2003) Cell , vol.114 , pp. 469-482
    • Xie, Z.1    Sanada, K.2    Samuels, B.A.3    Shih, H.4    Tsai, L.H.5
  • 60
    • 33748993710 scopus 로고    scopus 로고
    • Kinase activity of mutant LRRK2 mediates neuronal toxicity
    • Smith, W. W. et al. Kinase activity of mutant LRRK2 mediates neuronal toxicity. Nat. Neurosci. 9, 1231-1233 (2006).
    • (2006) Nat. Neurosci. , vol.9 , pp. 1231-1233
    • Smith, W.W.1
  • 61
    • 0141865509 scopus 로고    scopus 로고
    • Negative regulation of FAK signaling by SOCS proteins
    • Liu, E., Cote, J. F. & Vuori, K. Negative regulation of FAK signaling by SOCS proteins. EMBO J. 22, 5036-5046 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5036-5046
    • Liu, E.1    Cote, J.F.2    Vuori, K.3
  • 62
    • 0345593816 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts
    • Angers-Loustau, A. et al. Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts. J. Cell Biol. 144, 1019-1031 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 1019-1031
    • Angers-Loustau, A.1
  • 63
    • 0039441744 scopus 로고    scopus 로고
    • Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility
    • Manes, S. et al. Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility. Mol. Cell. Biol. 19, 3125-3135 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3125-3135
    • Manes, S.1
  • 64
    • 67649950283 scopus 로고    scopus 로고
    • FAK phosphorylation by ERK primes ras-induced tyrosine dephosphorylation of FAK mediated by PIN1 and PTP-PEST
    • Zheng, Y. et al. FAK phosphorylation by ERK primes ras-induced tyrosine dephosphorylation of FAK mediated by PIN1 and PTP-PEST. Mol. Cell 35, 11-25 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 11-25
    • Zheng, Y.1
  • 65
    • 84883168748 scopus 로고    scopus 로고
    • Pink1 deficiency attenuates astrocyte proliferation through mitochondrial dysfunction, reduced akt and increased p38 mapk activation, and downregulation EGFR
    • Choi, I. et al. Pink1 deficiency attenuates astrocyte proliferation through mitochondrial dysfunction, reduced akt and increased p38 mapk activation, and downregulation egfr. Glia 61, 800-812 (2013).
    • (2013) Glia , vol.61 , pp. 800-812
    • Choi, I.1
  • 66
    • 84883614843 scopus 로고    scopus 로고
    • DJ-1 facilitates the interaction between STAT1 and its phosphatase, SHP-1, in brain microglia and astrocytes: A novel antiinflammatory function of DJ-1
    • Kim, J. H. et al. DJ-1 facilitates the interaction between STAT1 and its phosphatase, SHP-1, in brain microglia and astrocytes: a novel antiinflammatory function of DJ-1. Neurobiol. Dis 60C, 1-10 (2013).
    • (2013) Neurobiol. Dis , vol.C60 , pp. 1-10
    • Kim, J.H.1
  • 67
    • 84887563272 scopus 로고    scopus 로고
    • DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes
    • Kim, K. S. et al. DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes. Hum. Mol. Genet 22, 4805-4817 (2013).
    • (2013) Hum. Mol. Genet , vol.22 , pp. 4805-4817
    • Kim, K.S.1
  • 68
    • 84918501910 scopus 로고    scopus 로고
    • Suppression of miR-155 expression in IFN-?-Treated astrocytes and microglia by DJ-1: A possible mechanism for maintaining SOCS1 expression
    • Kim, J. H. et al. Suppression of miR-155 expression in IFN-?-Treated astrocytes and microglia by DJ-1: a possible mechanism for maintaining SOCS1 expression. Exp. Neurobiol 23, 148-154 (2014).
    • (2014) Exp. Neurobiol , vol.23 , pp. 148-154
    • Kim, J.H.1
  • 69
    • 67649813448 scopus 로고    scopus 로고
    • Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinsons disease
    • Li, Y. et al. Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinsons disease. Nat. Neurosci. 12, 826-828 (2009).
    • (2009) Nat. Neurosci. , vol.12 , pp. 826-828
    • Li, Y.1
  • 70
    • 0032579949 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activated by lipopolysaccharide and beta-amyloid in cultured rat microglia
    • Pyo, H., Jou, I., Jung, S., Hong, S. & Joe, E. H. Mitogen-activated protein kinases activated by lipopolysaccharide and beta-amyloid in cultured rat microglia. Neuroreport 9, 871-874 (1998).
    • (1998) Neuroreport , vol.9 , pp. 871-874
    • Pyo, H.1    Jou, I.2    Jung, S.3    Hong, S.4    Joe, E.H.5
  • 71
    • 84903372586 scopus 로고    scopus 로고
    • Migration of neutrophils targeting amyloid plaques in Alzheimers disease mouse model
    • Baik, S. H. et al. Migration of neutrophils targeting amyloid plaques in Alzheimers disease mouse model. Neurobiol. Aging 35, 1286-1292 (2014).
    • (2014) Neurobiol. Aging , vol.35 , pp. 1286-1292
    • Baik, S.H.1


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