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Volumn 6, Issue , 2016, Pages

Optogenetic clustering of CNK1 reveals mechanistic insights in RAF and AKT signalling controlling cell fate decisions

Author keywords

[No Author keywords available]

Indexed keywords

CNKSR1 PROTEIN, HUMAN; PROTEIN KINASE B; RAF PROTEIN; SIGNAL PEPTIDE;

EID: 84999851956     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep38155     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: Hubs for controlling the flow of cellular information
    • Good, M. C., Zalatan, J. G., Lim, W. A. Scaffold proteins: hubs for controlling the flow of cellular information. Science 332, 680-6 (2011).
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 2
    • 34248576576 scopus 로고    scopus 로고
    • KSR and CNK: Two scaffolds regulating RAS-mediated RAF activation
    • Clapéron, a., Therrien, M. KSR and CNK: two scaffolds regulating RAS-mediated RAF activation. Oncogene 26, 3143-58 (2007).
    • (2007) Oncogene , vol.26 , pp. 3143-3158
    • Clapéron, A.1    Therrien, M.2
  • 4
    • 0842325725 scopus 로고    scopus 로고
    • Linking rho and ras signal transduction pathways
    • Human CNK1 Acts as a Scaffold Protein
    • Jaffe, A. B., Aspenstro, P., Hall, A. Human CNK1 Acts as a Scaffold Protein, Linking Rho and Ras Signal Transduction Pathways. Mol. Cell Biol. 24, 1736-1746 (2004).
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1736-1746
    • Jaffe, A.B.1    Aspenstro, P.2    Hall, A.3
  • 5
    • 14744276941 scopus 로고    scopus 로고
    • Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho
    • Jaffe, A. B., Hall, A., Schmidt, A. Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho. Curr. Biol. 15, 405-12 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 405-412
    • Jaffe, A.B.1    Hall, A.2    Schmidt, A.3
  • 6
    • 21244463565 scopus 로고    scopus 로고
    • CNK1 is a scaffold protein that regulates Src-mediated Raf-1 activation
    • Ziogas, A., Moelling, K., Radziwill, G. CNK1 is a scaffold protein that regulates Src-mediated Raf-1 activation. J. Biol. Chem. 280, 24205-11 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 24205-24211
    • Ziogas, A.1    Moelling, K.2    Radziwill, G.3
  • 7
    • 77953809690 scopus 로고    scopus 로고
    • CNK1 is a novel Akt interaction partner that promotes cell proliferation through the Akt-FoxO signalling axis
    • Fritz, R. D., Varga, Z., Radziwill, G. CNK1 is a novel Akt interaction partner that promotes cell proliferation through the Akt-FoxO signalling axis. Oncogene 29, 3575-82 (2010).
    • (2010) Oncogene , vol.29 , pp. 3575-3582
    • Fritz, R.D.1    Varga, Z.2    Radziwill, G.3
  • 8
    • 77949721038 scopus 로고    scopus 로고
    • CNK1 promotes invasion of cancer cells through NF-kappaB-dependent signaling
    • Fritz, R. D., Radziwill, G. CNK1 promotes invasion of cancer cells through NF-kappaB-dependent signaling. Mol. Cancer Res. 8, 395-406 (2010).
    • (2010) Mol. Cancer Res. , vol.8 , pp. 395-406
    • Fritz, R.D.1    Radziwill, G.2
  • 9
    • 77954852559 scopus 로고    scopus 로고
    • The CNK1 scaffold binds cytohesins and promotes insulin pathway signaling
    • Lim, J., Zhou, M., Veenstra, T. D., Morrison, D. K. The CNK1 scaffold binds cytohesins and promotes insulin pathway signaling. Genes Dev. 1496-1506 (2010).
    • (2010) Genes Dev. , vol.1496-1506
    • Lim, J.1    Zhou, M.2    Veenstra, T.D.3    Morrison, D.K.4
  • 10
    • 84940828287 scopus 로고    scopus 로고
    • Differential tyrosine phosphorylation controls the function of CNK1 as a molecular switch in signal transduction
    • Fischer, A., Brummer, T., Warscheid, B., Radziwill, G. Differential tyrosine phosphorylation controls the function of CNK1 as a molecular switch in signal transduction. Biochim. Biophys. Acta-Mol. Cell Res. 1853, 2847-2855 (2015).
    • (2015) Biochim. Biophys. Acta-Mol. Cell Res. , vol.1853 , pp. 2847-2855
    • Fischer, A.1    Brummer, T.2    Warscheid, B.3    Radziwill, G.4
  • 11
    • 84904995490 scopus 로고    scopus 로고
    • Illuminating cell signalling with optogenetic tools
    • Tischer, D., Weiner, O. D. Illuminating cell signalling with optogenetic tools. Nat. Rev. Mol. Cell Biol. 15, 551-8 (2014).
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 551-558
    • Tischer, D.1    Weiner, O.D.2
  • 12
    • 84922638213 scopus 로고    scopus 로고
    • Optogenetic control of signaling in mammalian cells
    • Beyer, H. M., Naumann, S., Weber, W., Radziwill, G. Optogenetic control of signaling in mammalian cells. Biotechnol. J. 10, 273-83 (2015).
    • (2015) Biotechnol. J. , vol.10 , pp. 273-283
    • Beyer, H.M.1    Naumann, S.2    Weber, W.3    Radziwill, G.4
  • 13
    • 78649714869 scopus 로고    scopus 로고
    • Rapid blue light induction of protein interaction in living cells
    • Kennedy, M. J. et al. Rapid blue light induction of protein interaction in living cells. Nat. Methods 7, 973-975 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 973-975
    • Kennedy, M.J.1
  • 14
    • 84874656353 scopus 로고    scopus 로고
    • Optogenetic protein clustering and signaling activation in mammalian cells
    • Bugaj, L. J., Choksi, A. T., Mesuda, C. K., Kane, R. S., Schaffer, D. V. Optogenetic protein clustering and signaling activation in mammalian cells. Nat. Methods 10, 249-252 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 249-252
    • Bugaj, L.J.1    Choksi, A.T.2    Mesuda, C.K.3    Kane, R.S.4    Schaffer, D.V.5
  • 15
    • 84908520377 scopus 로고    scopus 로고
    • An optimized optogenetic clustering tool for probing protein interaction and function
    • Taslimi, A. et al. An optimized optogenetic clustering tool for probing protein interaction and function. Nat. Commun. 5, 4925 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4925
    • Taslimi, A.1
  • 16
    • 84900874407 scopus 로고    scopus 로고
    • Optogenetic control of protein kinase activity in mammalian cells
    • Wend, S. et al. Optogenetic control of protein kinase activity in mammalian cells. ACS Synth. Biol. 3, 280-5 (2014).
    • (2014) ACS Synth. Biol. , vol.3 , pp. 280-285
    • Wend, S.1
  • 17
    • 84962449962 scopus 로고    scopus 로고
    • Optogenetically controlled RAF to characterize BRAF and CRAF protein kinase inhibitors
    • Chatelle, C. V. et al. Optogenetically controlled RAF to characterize BRAF and CRAF protein kinase inhibitors. Sci. Rep. 6, 23713 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 23713
    • Chatelle, C.V.1
  • 18
    • 84904568275 scopus 로고    scopus 로고
    • Spatiotemporal control of fibroblast growth factor receptor signals by blue light
    • Kim, N. et al. Spatiotemporal Control of Fibroblast Growth Factor Receptor Signals by Blue Light. Chem. Biol. 21, 903-912 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 903-912
    • Kim, N.1
  • 19
    • 84928807371 scopus 로고    scopus 로고
    • Regulation of endogenous transmembrane receptors through optogenetic Cry2 clustering
    • Bugaj, L. J. et al. Regulation of endogenous transmembrane receptors through optogenetic Cry2 clustering. Nat. Commun. 6, 6898 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 6898
    • Bugaj, L.J.1
  • 20
    • 0035816691 scopus 로고    scopus 로고
    • Differential usage of signal transduction pathways defines two types of serum response factor target gene
    • Gineitis, D., Treisman, R. Differential usage of signal transduction pathways defines two types of serum response factor target gene. J. Biol. Chem. 276, 24531-9 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24531-24539
    • Gineitis, D.1    Treisman, R.2
  • 21
    • 84947023702 scopus 로고    scopus 로고
    • A positive feedback loop between Akt and mTORC2 via SIN1 phosphorylation
    • Yang, G., Murashige, D. S., Humphrey, S. J., James, D. E. A Positive Feedback Loop between Akt and mTORC2 via SIN1 Phosphorylation. Cell Rep. 12, 937-43 (2015).
    • (2015) Cell Rep. , vol.12 , pp. 937-943
    • Yang, G.1    Murashige, D.S.2    Humphrey, S.J.3    James, D.E.4
  • 22
    • 33645520353 scopus 로고    scopus 로고
    • A KSR/CNK complex mediated by HYP, a novel SAM domain-containing protein, regulates RAS-dependent RAF activation in Drosophila
    • Douziech, M., Sahmi, M., Laberge, G., Therrien, M. A KSR/CNK complex mediated by HYP, a novel SAM domain-containing protein, regulates RAS-dependent RAF activation in Drosophila. Genes Dev. 3, 807-819 (2006).
    • (2006) Genes Dev. , vol.3 , pp. 807-819
    • Douziech, M.1    Sahmi, M.2    Laberge, G.3    Therrien, M.4
  • 23
    • 33645521412 scopus 로고    scopus 로고
    • The novel SAM domain protein Aveugle is required for Raf activation in the Drosophila EGF receptor signaling pathway
    • Roignant, J., Hamel, S., Janody, F., Treisman, J. E. The novel SAM domain protein Aveugle is required for Raf activation in the Drosophila EGF receptor signaling pathway. Genes Dev. 795-806 (2006).
    • (2006) Genes Dev. , pp. 795-806
    • Roignant, J.1    Hamel, S.2    Janody, F.3    Treisman, J.E.4
  • 24
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann, S., Moelling, K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286, 1741-1744 (1999).
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 25
    • 38049147787 scopus 로고    scopus 로고
    • MEF2: A central regulator of diverse developmental programs
    • Potthoff, M. J., Olson, E. N. MEF2: a central regulator of diverse developmental programs. Development 134, 4131-40 (2007).
    • (2007) Development , vol.134 , pp. 4131-4140
    • Potthoff, M.J.1    Olson, E.N.2
  • 26
    • 23944498100 scopus 로고    scopus 로고
    • The spot 14 protein inhibits growth and induces differentiation and cell death of human MCF-7 breast cancer cells
    • Sanchez-Rodriguez, J., Kaninda-Tshilumbu, J. P., Santos, A., Perez-Castillo, A. The spot 14 protein inhibits growth and induces differentiation and cell death of human MCF-7 breast cancer cells. Biochem. J. 390, 57-65 (2005).
    • (2005) Biochem. J. , vol.390 , pp. 57-65
    • Sanchez-Rodriguez, J.1    Kaninda-Tshilumbu, J.P.2    Santos, A.3    Perez-Castillo, A.4
  • 27
    • 0021923858 scopus 로고
    • Nile red: A selective fluorescent stain for intracellular lipid droplets
    • Greenspan, P. Nile red: a selective fluorescent stain for intracellular lipid droplets. J. Cell Biol. 100, 965-973 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 965-973
    • Greenspan, P.1
  • 28
    • 84887040380 scopus 로고    scopus 로고
    • Transforming growth factor-? Signalling controls human breast cancer metastasis in a zebrafish xenograft model
    • Drabsch, Y. et al. Transforming growth factor-? signalling controls human breast cancer metastasis in a zebrafish xenograft model. Breast Cancer Res. 15, 10-16 (2013).
    • (2013) Breast Cancer Res. , vol.15 , pp. 10-16
    • Drabsch, Y.1
  • 30
    • 0035823542 scopus 로고    scopus 로고
    • Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells
    • Reusch, H. P., Zimmermann, S., Schaefer, M., Paul, M., Moelling, K. Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells. J. Biol. Chem. 276, 33630-7 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 33630-33637
    • Reusch, H.P.1    Zimmermann, S.2    Schaefer, M.3    Paul, M.4    Moelling, K.5
  • 31
    • 84863241921 scopus 로고    scopus 로고
    • Signaling network crosstalk in human pluripotent cells: A Smad2/3-regulated switch that controls the balance between self-renewal and differentiation
    • Singh, A. M. et al. Signaling network crosstalk in human pluripotent cells: a Smad2/3-regulated switch that controls the balance between self-renewal and differentiation. Cell Stem Cell 10, 312-26 (2012).
    • (2012) Cell Stem Cell , vol.10 , pp. 312-326
    • Singh, A.M.1
  • 32
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • Rommel, C. et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 286, 1738-41 (1999).
    • (1999) Science , vol.286 , pp. 1738-1741
    • Rommel, C.1
  • 34
    • 84874915869 scopus 로고    scopus 로고
    • It takes two to tango-signalling by dimeric Raf kinases
    • Baljuls, A., Kholodenko, B. N., Kolch, W. It takes two to tango-signalling by dimeric Raf kinases. Mol. Biosyst. 9, 551-8 (2013).
    • (2013) Mol. Biosyst. , vol.9 , pp. 551-558
    • Baljuls, A.1    Kholodenko, B.N.2    Kolch, W.3
  • 35
    • 84929077789 scopus 로고    scopus 로고
    • Regulation of RAF protein kinases in ERK signalling
    • Lavoie, H., Therrien, M. Regulation of RAF protein kinases in ERK signalling. Nat. Rev. Mol. Cell Biol. 16, 281-298 (2015).
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 281-298
    • Lavoie, H.1    Therrien, M.2
  • 36
    • 0034282892 scopus 로고    scopus 로고
    • Negative regulation of the serine/threonine kinase B-Raf by Akt
    • Guan, K. L. et al. Negative regulation of the serine/threonine kinase B-Raf by Akt. J. Biol. Chem. 275, 27354-9 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27354-27359
    • Guan, K.L.1
  • 37
    • 84947023702 scopus 로고    scopus 로고
    • A Positive Feedback Loop between Akt and mTORC2 via SIN1 Phosphorylation
    • Yang, G., Murashige, D. S., Humphrey, S. J., James, D. E. A Positive Feedback Loop between Akt and mTORC2 via SIN1 Phosphorylation. Cell Rep. 12, 937-43 (2015).
    • (2015) Cell Rep. , vol.12 , pp. 937-943
    • Yang, G.1    Murashige, D.S.2    Humphrey, S.J.3    James, D.E.4
  • 39
    • 15644381754 scopus 로고    scopus 로고
    • Role of translocation in the activation and function of protein kinase B
    • Andjelkovi?, M. et al. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-24 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31515-31524
    • Andjelkovi, M.1
  • 40
    • 0035914338 scopus 로고    scopus 로고
    • Insulin-like Growth Factor-mediated Muscle Differentiation: Collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenein
    • Tureckova, J., Wilson, E. M., Cappalonga, J. L., Rotwein, P. Insulin-like Growth Factor-mediated Muscle Differentiation: collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenein. J. Biol. Chem. 276, 39264-39270 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 39264-39270
    • Tureckova, J.1    Wilson, E.M.2    Cappalonga, J.L.3    Rotwein, P.4
  • 41
    • 30344442873 scopus 로고    scopus 로고
    • The many faces of SAM
    • Qiao, F., Bowie, J. U. The many faces of SAM. Sci. STKE 2005, re7 (2005).
    • (2005) Sci. STKE , vol.2005 , pp. 7
    • Qiao, F.1    Bowie, J.U.2
  • 42
    • 84999752561 scopus 로고    scopus 로고
    • AKT-dependent phosphorylation of the SAM domain induces oligomerization and activation of the scaffold protein CNK1
    • In press
    • Fischer, A., Weber, W., Warscheid, B., Radziwill, G. AKT-dependent phosphorylation of the SAM domain induces oligomerization and activation of the scaffold protein CNK1. Biochim. Biophys. Acta In press (2016).
    • (2016) Biochim. Biophys. Acta
    • Fischer, A.1    Weber, W.2    Warscheid, B.3    Radziwill, G.4
  • 43
    • 0035943615 scopus 로고    scopus 로고
    • Serum-and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf
    • Zhang, B. H. et al. Serum-and Glucocorticoid-inducible Kinase SGK Phosphorylates and Negatively Regulates B-Raf. J. Biol. Chem. 276, 31620-31626 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 31620-31626
    • Zhang, B.H.1
  • 44
    • 61849087361 scopus 로고    scopus 로고
    • Regulation of human myoblast differentiation by PEBP4
    • Garcia, R., Grindlay, J., Rath, O., Fee, F., Kolch, W. Regulation of human myoblast differentiation by PEBP4. EMBO Rep. 10, 278-84 (2009).
    • (2009) EMBO Rep. , vol.10 , pp. 278-284
    • Garcia, R.1    Grindlay, J.2    Rath, O.3    Fee, F.4    Kolch, W.5
  • 45
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch, W. Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6, 827-37 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 46
    • 84943595596 scopus 로고    scopus 로고
    • Crosstalk between MAPK/ERK and PI3K/AKT signal pathways during brain ischemia/reperfusion
    • Zhou, J. et al. Crosstalk Between MAPK/ERK and PI3K/AKT Signal Pathways During Brain Ischemia/Reperfusion. ASN Neuro 7 (2015).
    • (2015) ASN Neuro , vol.7
    • Zhou, J.1
  • 47
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • Alessi, D. R. et al. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 15, 6541-51 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6541-6551
    • Alessi, D.R.1
  • 48
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson, D. G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343-5 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1


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