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Volumn 111, Issue 34, 2014, Pages 12420-12425

Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms

Author keywords

Image analysis; Live cell imaging; Motion classification; Protein engineering; Rapamycin

Indexed keywords

FK 506 BINDING PROTEIN; ISOPROTEIN; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN KINASE YES; PROTEIN SH3; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE SHP; RAPAMYCIN; HYBRID PROTEIN; ISOENZYME;

EID: 84906679884     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1404487111     Document Type: Article
Times cited : (47)

References (48)
  • 1
    • 0017250977 scopus 로고
    • DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
    • Stehelin D, Varmus HE, Bishop JM, Vogt PK (1976) DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA. Nature 260(5547):170-173.
    • (1976) Nature , vol.260 , Issue.5547 , pp. 170-173
    • Stehelin, D.1    Varmus, H.E.2    Bishop, J.M.3    Vogt, P.K.4
  • 2
    • 0028170518 scopus 로고
    • Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice
    • Stein PL, Vogel H, Soriano P (1994) Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice. Genes Dev 8(17):1999-2007.
    • (1994) Genes Dev , vol.8 , Issue.17 , pp. 1999-2007
    • Stein, P.L.1    Vogel, H.2    Soriano, P.3
  • 4
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • Lowell CA, Soriano P (1996) Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories. Genes Dev 10(15):1845-1857. (Pubitemid 26281680)
    • (1996) Genes and Development , vol.10 , Issue.15 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 5
    • 0029093295 scopus 로고
    • Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division
    • Roche S, Fumagalli S, Courtneidge SA (1995) Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division. Science 269(5230):1567-1569.
    • (1995) Science , vol.269 , Issue.5230 , pp. 1567-1569
    • Roche, S.1    Fumagalli, S.2    Courtneidge, S.A.3
  • 6
    • 33644595058 scopus 로고    scopus 로고
    • Src, Fyn and Yes play differential roles in VEGF-mediated endothelial cell events
    • Werdich XQ, Penn JS (2005) Src, Fyn and Yes play differential roles in VEGF-mediated endothelial cell events. Angiogenesis 8(4):315-326.
    • (2005) Angiogenesis , vol.8 , Issue.4 , pp. 315-326
    • Werdich, X.Q.1    Penn, J.S.2
  • 7
    • 71949115354 scopus 로고    scopus 로고
    • Transforming potential of Src family kinases is limited by the cholesterol-enriched membrane microdomain
    • Oneyama C, et al. (2009) Transforming potential of Src family kinases is limited by the cholesterol-enriched membrane microdomain. Mol Cell Biol 29(24):6462-6472.
    • (2009) Mol Cell Biol , vol.29 , Issue.24 , pp. 6462-6472
    • Oneyama, C.1
  • 8
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh MD (1994) Myristylation and palmitylation of Src family members: The fats of the matter. Cell 76(3):411-413.
    • (1994) Cell , vol.76 , Issue.3 , pp. 411-413
    • Resh, M.D.1
  • 9
    • 79955632219 scopus 로고    scopus 로고
    • Differential transformation capacity of Src family kinases during the initiation of prostate cancer
    • Cai H, et al. (2011) Differential transformation capacity of Src family kinases during the initiation of prostate cancer. Proc Natl Acad Sci USA 108(16):6579-6584.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.16 , pp. 6579-6584
    • Cai, H.1
  • 10
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • DOI 10.1083/jcb.135.6.1551
    • Fincham VJ, et al. (1996) Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J Cell Biol 135(6 Pt 1):1551-1564. (Pubitemid 26427651)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.G.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 13
    • 66849087348 scopus 로고    scopus 로고
    • Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain
    • Sato I, et al. (2009) Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain. J Cell Sci 122(Pt 7):965-975.
    • (2009) J Cell Sci , vol.122 , Issue.PART 7 , pp. 965-975
    • Sato, I.1
  • 14
    • 34548282678 scopus 로고    scopus 로고
    • The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements
    • DOI 10.1242/jcs.003657
    • Sandilands E, Brunton VG, Frame MC (2007) The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements. J Cell Sci 120(Pt 15):2555-2564. (Pubitemid 47323864)
    • (2007) Journal of Cell Science , vol.120 , Issue.15 , pp. 2555-2564
    • Sandilands, E.1    Brunton, V.G.2    Frame, M.C.3
  • 15
    • 78149369733 scopus 로고    scopus 로고
    • Comparative analysis of human SRC-family kinase substrate specificity in vitro
    • Takeda H, et al. (2010) Comparative analysis of human SRC-family kinase substrate specificity in vitro. J Proteome Res 9(11):5982-5993.
    • (2010) J Proteome Res , vol.9 , Issue.11 , pp. 5982-5993
    • Takeda, H.1
  • 16
    • 0036008093 scopus 로고    scopus 로고
    • A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway
    • DOI 10.1016/S1074-5521(02)00086-8, PII S1074552102000868
    • Shah K, Shokat KM (2002) A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway. Chem Biol 9(1):35-47. (Pubitemid 34155863)
    • (2002) Chemistry and Biology , vol.9 , Issue.1 , pp. 35-47
    • Shah, K.1    Shokat, K.M.2
  • 17
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown MT, Cooper JA (1996) Regulation, substrates and functions of Src. Biochim Biophys Acta 1287(2-3):121- 149.
    • (1996) Biochim Biophys Acta , vol.1287 , Issue.2-3 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 18
    • 0029045815 scopus 로고
    • Specific and redundant roles of Src and Fyn in organizing the cytoskeleton
    • Thomas SM, Soriano P, Imamoto A (1995) Specific and redundant roles of Src and Fyn in organizing the cytoskeleton. Nature 376(6537):267-271.
    • (1995) Nature , vol.376 , Issue.6537 , pp. 267-271
    • Thomas, S.M.1    Soriano, P.2    Imamoto, A.3
  • 20
    • 84858326787 scopus 로고    scopus 로고
    • Allosteric activation of kinases: Design and application of RapR kinases
    • (Wiley, New York) Chap 14, unit 13
    • Karginov AV, Hahn KM (2011) Allosteric activation of kinases: Design and application of RapR kinases. Current Protocols in Cell Biology (Wiley, New York) Chap 14, unit 13.
    • (2011) Current Protocols in Cell Biology
    • Karginov, A.V.1    Hahn, K.M.2
  • 21
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski R, Jr (2004) Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 324(4):1155-1164.
    • (2004) Biochem Biophys Res Commun , vol.324 , Issue.4 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 22
    • 84897021544 scopus 로고    scopus 로고
    • Dissecting motility signaling through activation of specific Src-effector complexes
    • Karginov AV, et al. (2014) Dissecting motility signaling through activation of specific Src-effector complexes. Nat Chem Biol 10(4):286-290.
    • (2014) Nat Chem Biol , vol.10 , Issue.4 , pp. 286-290
    • Karginov, A.V.1
  • 23
    • 84876882853 scopus 로고    scopus 로고
    • Rational design of a ligand-controlled protein conformational switch
    • Dagliyan O, et al. (2013) Rational design of a ligand-controlled protein conformational switch. Proc Natl Acad Sci USA 110(17):6800- 6804.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.17 , pp. 6800-6804
    • Dagliyan, O.1
  • 25
    • 0037150728 scopus 로고    scopus 로고
    • Src in cancer: Deregulation and consequences for cell behaviour
    • Frame MC (2002) Src in cancer: deregulation and consequences for cell behaviour. Biochim Biophys Acta 1602(2):114-130.
    • (2002) Biochim Biophys Acta , vol.1602 , Issue.2 , pp. 114-130
    • Frame, M.C.1
  • 26
    • 0038386613 scopus 로고    scopus 로고
    • Src family kinases in tumor progression and metastasis
    • DOI 10.1023/A:1023772912750
    • Summy JM, Gallick GE (2003) Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 22(4):337-358. (Pubitemid 36791891)
    • (2003) Cancer and Metastasis Reviews , vol.22 , Issue.4 , pp. 337-358
    • Summy, J.M.1    Gallick, G.E.2
  • 27
    • 76149110432 scopus 로고    scopus 로고
    • Roles of Fyn in pancreatic cancer metastasis
    • Chen ZY, et al. (2010) Roles of Fyn in pancreatic cancer metastasis. J Gastroenterol Hepatol 25(2):293-301.
    • (2010) J Gastroenterol Hepatol , vol.25 , Issue.2 , pp. 293-301
    • Chen, Z.Y.1
  • 28
    • 0025765803 scopus 로고
    • SH2 and SH3 Domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch CA, Anderson D, Moran MF, Ellis C, Pawson T (1991) SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252(5006):668-674. (Pubitemid 21916987)
    • (1991) Science , vol.252 , Issue.5006 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 29
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Songyang Z, Cantley LC (1995) Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem Sci 20(11):470-475.
    • (1995) Trends Biochem Sci , vol.20 , Issue.11 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 31
    • 0034610775 scopus 로고    scopus 로고
    • The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes
    • Summy JM, Guappone AC, Sudol M, Flynn DC (2000) The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes. Oncogene 19(1):155-160. (Pubitemid 30066362)
    • (2000) Oncogene , vol.19 , Issue.1 , pp. 155-160
    • Summy, J.M.1    Guappone, A.C.2    Sudol, M.3    Flynn, D.C.4
  • 32
    • 48649101763 scopus 로고    scopus 로고
    • A traffic-activated Golgi-based signalling circuit coordinates the secretory pathway
    • Pulvirenti T, et al. (2008) A traffic-activated Golgi-based signalling circuit coordinates the secretory pathway. Nat Cell Biol 10(8):912-922.
    • (2008) Nat Cell Biol , vol.10 , Issue.8 , pp. 912-922
    • Pulvirenti, T.1
  • 33
    • 0028301606 scopus 로고
    • Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization
    • Alland L, Peseckis SM, Atherton RE, Berthiaume L, Resh MD (1994) Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization. J Biol Chem 269(24):16701-16705.
    • (1994) J Biol Chem , vol.269 , Issue.24 , pp. 16701-16705
    • Alland, L.1    Peseckis, S.M.2    Atherton, R.E.3    Berthiaume, L.4    Resh, M.D.5
  • 34
    • 0030613520 scopus 로고    scopus 로고
    • Palmitoylation of p59(fyn) is reversible and sufficient for plasma membrane association
    • Wolven A, Okamura H, Rosenblatt Y, Resh MD (1997) Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association. Mol Biol Cell 8(6):1159-1173. (Pubitemid 27276333)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.6 , pp. 1159-1173
    • Wolven, A.1    Okamura, H.2    Rosenblatt, Y.3    Resh, M.D.4
  • 35
    • 0027986678 scopus 로고
    • Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif
    • KoeglM, Zlatkine P, Ley SC, Courtneidge SA, Magee AI (1994) Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif. Biochem J 303(Pt 3):749-753. (Pubitemid 24326006)
    • (1994) Biochemical Journal , vol.303 , Issue.3 , pp. 749-753
    • Koegl, M.1    Zlatkine, P.2    Ley, S.C.3    Courtneidge, S.A.4    Magee, A.I.5
  • 36
    • 0033045090 scopus 로고    scopus 로고
    • Regional regulation of microtubule dynamics in polarized, motile cells
    • Wadsworth P (1999) Regional regulation of microtubule dynamics in polarized, motile cells. Cell Motil Cytoskeleton 42(1):48-59.
    • (1999) Cell Motil Cytoskeleton , vol.42 , Issue.1 , pp. 48-59
    • Wadsworth, P.1
  • 38
    • 0344034726 scopus 로고    scopus 로고
    • Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge
    • DOI 10.1242/jcs.00748
    • Schmoranzer J, Kreitzer G, Simon SM (2003) Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge. J Cell Sci 116(Pt 22):4513-4519. (Pubitemid 37461606)
    • (2003) Journal of Cell Science , vol.116 , Issue.22 , pp. 4513-4519
    • Schmoranzer, J.1    Kreitzer, G.2    Simon, S.M.3
  • 40
    • 0037483090 scopus 로고    scopus 로고
    • The SH4-Unique-SH3-SH2 domains dictate specificity in signaling that differentiate c-Yes from c-Src
    • Summy JM, et al. (2003) The SH4-Unique-SH3-SH2 domains dictate specificity in signaling that differentiate c-Yes from c-Src. J Cell Sci 116(Pt 12):2585 -2598.
    • (2003) J Cell Sci , vol.116 , Issue.PART 12 , pp. 2585-2598
    • Summy, J.M.1
  • 41
    • 84874322166 scopus 로고    scopus 로고
    • Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism
    • Pérez Y, et al. (2013) Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism. Sci Rep 3:1295.
    • (2013) Sci Rep , vol.3 , pp. 1295
    • Pérez, Y.1
  • 42
    • 0034941053 scopus 로고    scopus 로고
    • c-src and related tyrosine kinases: A role in the assembly and reorganization of matrix adhesions
    • Volberg T, Romer L, Zamir E, Geiger B (2001) pp60(c-src) and related tyrosine kinases: A role in the assembly and reorganization of matrix adhesions. J Cell Sci 114(Pt 12):2279-2289. (Pubitemid 32633699)
    • (2001) Journal of Cell Science , vol.114 , Issue.12 , pp. 2279-2289
    • Volberg, T.1    Romer, L.2    Zamir, E.3    Geiger, B.4
  • 44
    • 79960334368 scopus 로고    scopus 로고
    • High-resolution quantification of focal adhesion spatiotemporal dynamics in living cells
    • Berginski ME, Vitriol EA, Hahn KM, Gomez SM (2011) High-resolution quantification of focal adhesion spatiotemporal dynamics in living cells. PLoS ONE 6(7):e22025.
    • (2011) PLoS ONE , vol.6 , Issue.7
    • Berginski, M.E.1    Vitriol, E.A.2    Hahn, K.M.3    Gomez, S.M.4
  • 45
    • 7944237784 scopus 로고    scopus 로고
    • The interplay between Src family kinases and receptor tyrosine kinases
    • DOI 10.1038/sj.onc.1208079
    • Bromann PA, Korkaya H, Courtneidge SA (2004) The interplay between Src family kinases and receptor tyrosine kinases. Oncogene 23(48):7957-7968. (Pubitemid 39468854)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7957-7968
    • Bromann, P.A.1    Korkaya, H.2    Courtneidge, S.A.3
  • 46
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • DOI 10.1038/sj.onc.1208080
    • Playford MP, Schaller MD (2004) The interplay between Src and integrins in normal and tumor biology. Oncogene 23(48):7928-7946. (Pubitemid 39468852)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 47
    • 0020685571 scopus 로고
    • Characterising a kinesis response: Time averaged measures of cell speed and directional persistence
    • Dunn GA (1983) Characterising a kinesis response: Time averaged measures of cell speed and directional persistence. Agents Actions Suppl 12:14-33.
    • (1983) Agents Actions Suppl , vol.12 , pp. 14-33
    • Dunn, G.A.1
  • 48
    • 0023746235 scopus 로고
    • Models of dispersal in biological systems
    • Othmer HG, Dunbar SR, Alt W (1988) Models of dispersal in biological systems. J Math Biol 26(3):263-298.
    • (1988) J Math Biol , vol.26 , Issue.3 , pp. 263-298
    • Othmer, H.G.1    Dunbar, S.R.2    Alt, W.3


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