Differential tyrosine phosphorylation controls the function of CNK1 as a molecular switch in signal transduction

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1853, Issue 11, 2015, Pages 2847-2855

  Fischer, Adrian ^a   Brummer, Tilman ^a   Warscheid, Bettina ^a   Radziwill, Gerald ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

CNK1; Platelet derived growth factor; Scaffold protein; Signal transduction; SRC; Tyrosine phosphorylation

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MATRIX METALLOPROTEINASE 14; PHOSPHATIDYLINOSITOL 3 KINASE; PLATELET DERIVED GROWTH FACTOR; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; SCAFFOLD PROTEIN; SCAFFOLD PROTEIN CNK1; TYROSINE; UNCLASSIFIED DRUG; CNKSR1 PROTEIN, HUMAN; MMP14 PROTEIN, HUMAN; SIGNAL PEPTIDE;

ARTICLE; CELL INVASION; CELL MEMBRANE; CELL NUCLEUS; CELL PROLIFERATION; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; DIMERIZATION; FEMALE; GENE EXPRESSION; GENE SILENCING; GENE SWITCHING; HELA CELL LINE; HUMAN; HUMAN CELL; MASS SPECTROMETRY; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; BIOSYNTHESIS; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; HEK293 CELL LINE; METABOLISM; MUTATION; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN TRANSPORT;

CELL MEMBRANE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE KNOCKDOWN TECHNIQUES; HEK293 CELLS; HELA CELLS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MATRIX METALLOPROTEINASE 14; MUTATION; PHOSPHORYLATION; PROMOTER REGIONS, GENETIC; PROTEIN TRANSPORT; SRC-FAMILY KINASES; TYROSINE;

EID: 84940828287     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.08.014     Document Type: Article

References (26)

1. Good M.C., Zalatan J.G., Lim W.A. Scaffold proteins: hubs for controlling the flow of cellular information. Science 2011, 332:680-686.
2. Kolch W. Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 2005, 6:827-837.
3. Clapéron A., Therrien M. KSR and CNK: two scaffolds regulating RAS-mediated RAF activation. Oncogene 2007, 26:3143-3158.
4. Therrien M., Wong A.M., Rubin G.M. CNK, a RAF-binding multidomain protein required for RAS signaling. Cell 1998, 95:343-353.
5. Fritz R.D., Radziwill G. CNK1 and other scaffolds for Akt/FoxO signaling. Biochim. Biophys. Acta, Mol. Cell Res. 2011, 1813:1971-1977.
6. Lim J., Zhou M., Veenstra T.D., Morrison D.K. The CNK1 scaffold binds cytohesins and promotes insulin pathway signaling. Genes Dev. 2010, 24:1496-1506.
7. 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 2010, 29:3575-3582.
8. Jaffe A.B., Aspenström P., Hall A. Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways. Mol. Cell. Biol. 2004, 24:1736-1746.
9. Jaffe A.B., Hall A., Schmidt A. Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho. Curr. Biol. 2005, 15:405-412.
10. Fritz R.D., Radziwill G. CNK1 promotes invasion of cancer cells through NF-kappaB-dependent signaling. Mol. Cancer Res. 2010, 8:395-406.
11. Rabizadeh S., Xavier R.J., Ishiguro K., Bernabeortiz J., Lopez-Ilasaca M., Khokhlatchev A., Mollahan P., Pfeifer G.P., Avruch J., Seed B. The scaffold protein CNK1 interacts with the tumor suppressor RASSF1A and augments RASSF1A-induced cell death. J. Biol. Chem. 2004, 279:29247-29254.
12. Ziogas A., Moelling K., Radziwill G. CNK1 is a scaffold protein that regulates Src-mediated Raf-1 activation. J. Biol. Chem. 2005, 280:24205-24211.
13. Radziwill G., Weiss A., Heinrich J., Baumgartner M., Boisguerin P., Owada K., Moelling K. Regulation of c-Src by binding to the PDZ domain of AF-6. EMBO J. 2007, 26:2633-2644.
14. Wend S., Wagner H. Optogenetic control of protein kinase activity in mammalian cells. ACS Synth. Biol. 2014, 3:280-285.
15. Brummer T., Schramek D., Hayes V.M., Bennett H.L., Caldon C.E., Musgrove E.A., Daly R.J. Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein. J. Biol. Chem. 2006, 281:626-637.
16. Oeljeklaus S., Reinartz B.S., Wolf J., Wiese S., Tonillo J., Podwojski K., Kuhlmann K., Stephan C., Meyer H.E., Schliebs W., et al. Identification of core components and transient interactors of the peroxisomal importomer by dual-track stable isotope labeling with amino acids in cell culture analysis. J. Proteome Res. 2012, 11:2567-2580.
17. Wiese H., Gelis L., Wiese S., Reichenbach C., Jovancevic N., Osterloh M., Meyer H.E., Neuhaus E.M., Hatt H.H., Radziwill G., et al. Quantitative phosphoproteomics reveals the protein tyrosine kinase Pyk2 as a central effector of olfactory receptor signaling in prostate cancer cells. Biochim. Biophys. Acta 2014, 1854:632-640.
18. Lytovchenko O., Naumenko N., Oeljeklaus S., Schmidt B., von der Malsburg K., Deckers M., Warscheid B., van der Laan M., Rehling P. The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase. EMBO J. 2014, 33:1624-1638.
19. Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
20. DeMali K.A., Godwin S.L., Soltoff S.P., Kazlauskas A. Multiple roles for Src in a PDGF-stimulated cell. Exp. Cell Res. 1999, 253:271-279.
21. Demoulin J.-B., Essaghir A. PDGF receptor signaling networks in normal and cancer cells. Cytokine Growth Factor Rev. 2014, 25:273-283.
22. Twamley-Stein G.M., Pepperkok R., Ansorge W., Courtneidge S.A. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:7696-7700.
23. Rajakulendran T., Sahmi M., Kurinov I., Tyers M., Therrien M., Sicheri F. CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:2836-2841.
24. Fritz R.D., Radziwill G. The scaffold protein CNK1 interacts with the angiotensin II type 2 receptor. Biochem. Biophys. Res. Commun. 2005, 338:1906-1912.
25. Laberge G., Douziech M., Therrien M. Src42 binding activity regulates Drosophila RAF by a novel CNK-dependent derepression mechanism. EMBO J. 2005, 24:487-498.
26. Cho H.J., Hwang Y.-S., Mood K., Ji Y.J., Lim J., Morrison D.K., Daar I.O. EphrinB1 interacts with CNK1 and promotes cell migration through c-Jun N-terminal kinase (JNK) activation. J. Biol. Chem. 2014, 289:18556-18568.