ΠΠ€Π -Π·Π°Π²ΠΈΡΠΈΠΌΠ°Ρ ΠΏΠ΅ΡΠ΅Π΄Π°ΡΠ° ΡΠΈΠ³Π½Π°Π»Π° Ρ ΡΡΠ°ΡΡΠΈΠ΅ΠΌ ΡΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΡΠ°ΠΊΡΠΎΡΠ° STAT
ΠΠ΅ΡΠΌΠΎΡΡΡ Π½Π° ΡΠΎ, ΡΡΠΎ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΡΠ½Π΄ΠΎΡΠΈΡΠΎΠ·Π° ΠΠ€Π -ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Π²Π΅Π΄ΡΡΡΡ ΡΠΆΠ΅ Π½Π΅ ΠΎΠ΄Π½ΠΎ Π΄Π΅ΡΡΡΠΈΠ»Π΅ΡΠΈΠ΅, Π·Π½Π°ΡΠ΅Π½ΠΈΠ΅ ΡΡΠΎΠ³ΠΎ ΠΏΡΠΎΡΠ΅ΡΡΠ° Π΄Π»Ρ ΠΏΠ΅ΡΠ΅Π΄Π°ΡΠΈ ΡΠΈΠ³Π½Π°Π»Π° Π΄ΠΎ ΡΠΈΡ ΠΏΠΎΡ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΏΡΠ΅Π΄ΠΌΠ΅ΡΠΎΠΌ Π΄ΠΈΡΠΊΡΡΡΠΈΠΈ. ΠΡΡ ΠΎΠ΄Π½ΠΎ ΠΏΠΎΠ»Π°Π³Π°Π»ΠΈ, ΡΡΠΎ ΡΠ΄Π°Π»Π΅Π½ΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΡΡ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠΎΠ² Ρ ΠΏΠ»Π°Π·ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΈ ΠΏΠΎΡΠ»Π΅Π΄ΡΡΡΠ°Ρ ΠΈΡ Π΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΡ ΠΌΠΎΠΆΠ΅Ρ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡΡ ΠΊ ΡΠ½ΠΈΠΆΠ΅Π½ΠΈΡ ΡΠΈΠ³Π½Π°Π»Π°. ΠΠΎ Π±ΡΠ»ΠΎ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ ΠΈΠ½ΡΠ΅ΡΠ½Π°Π»ΠΈΠ·Π°ΡΠΈΠΈ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡ ΠΎΡΡΠ°Π΅ΡΡΡ… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- ΠΡΠ½Π°ΡΡΠΎΠ² A.M., ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H. ΠΠ€Π -ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΡΡΠ°Π½ΡΠΏΠΎΡΡ Π² ΡΠ΄ΡΠΎ Ρ42/Ρ44 ΠΠΠ Π ΡΡΠ΅Π±ΡΠ΅Ρ Π½Π°Π»ΠΈΡΠΈΡ ΠΈΠ½ΡΠ°ΠΊΡΠ½ΠΎΠ³ΠΎ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ°. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 1998. 40: 639−647.
- ΠΠΈΠ½ΠΎΠ³ΡΠ°Π΄ΠΎΠ²Π° H.A., ΠΠ΅ΡΡΠ΅ΡΠΎΠ² A.M., Π Π΅ΡΠ΅ΡΠ½ΠΈΠΊΠΎΠ²Π° Π. Π€., Π‘ΠΎΡΠΊΠΈΠ½ ΠΠ, ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H. ΠΠΌΠΌΡΠ½ΠΎΡΠ»ΡΠΎΡΠ΅ΡΡΠ΅Π½ΡΠ½ΠΎΠ΅ Π²ΡΡΠ²Π»Π΅Π½ΠΈΠ΅ ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠΎΠ² ΠΠ€Π Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ ΠΈΡ ΠΈΠ½ΡΠ΅ΡΠ½Π°Π»ΠΈΠ·Π°ΡΠΈΠΈ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Π431. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 1990. 32: 384−387.
- ΠΠΎΡΠ½ΠΈΠ»ΠΎΠ²Π° Π.Π‘., Π‘ΠΎΡΠΊΠΈΠ½ Π. Π., ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H. ΠΠΈΠ½Π°ΠΌΠΈΠΊΠ° ΠΊΠΎΠΌΠΏΠ°ΡΡΠΌΠ΅Π½ΡΠ°Π»ΠΈΠ·Π°ΡΠΈΠΈ ΡΠΏΠΈΠ΄Π΅ΡΠΌΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΡΠ°ΠΊΡΠΎΡΠ° ΡΠΎΡΡΠ° Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Π431. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 1987. 29: 904−910.
- ΠΠ΅ΡΡΠ΅ΡΠΎΠ² A.M., ΠΠ΄ΠΎΠ²ΠΈΠ½Π° Π. Π., ΠΠΎΡΠ½ΠΈΠ»ΠΎΠ²Π° Π. Π‘., ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H. ΠΡΡΠΌΠΎΠ΅ Π΄ΠΎΠΊΠ°Π·Π°ΡΠ΅Π»ΡΡΡΠ²ΠΎ ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΏΠΎ ΡΠΈΡΠΎΠ·ΠΈΠ½Ρ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠΎΠ² ΠΠ€Π , ΠΈΠ½ΡΠ΅ΡΠ½Π°Π»ΠΈΠ·ΠΎΠ²Π°Π½Π½ΡΡ Π² ΡΠ½Π΄ΠΎΡΠΎΠΌΠ°Ρ ΠΊΠ»Π΅ΡΠΎΠΊ Π431. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ 1991. 33: 26−31.
- ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H., Π‘ΠΎΡΠΊΠΈΠ½ Π. Π., Π‘ΠΎΡΠΎΠΊΠΈΠ½ Π. Π. ΠΠΏΠΈΠ΄Π΅ΡΠΌΠ°Π»ΡΠ½ΡΠΉ ΡΠ°ΠΊΡΠΎΡ ΡΠΎΡΡΠ°. 1987. Π. «ΠΠ°ΡΠΊΠ°». 200 Ρ.
- ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ H.H. STAT-ΠΏΡΡΡ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΠΈΠ³ΡΠ°Π»ΠΈΠ·Π°ΡΠΈΠΈ. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 1998. 40: 1050−1052.
- ΠΠΎΡΠΏΠ΅Π»ΠΎΠ² Π.Π., ΠΠΎΡΠΏΠ΅Π»ΠΎΠ²Π° Π’. Π., Π‘Π°Π²Π΅Π»ΡΠ΅Π² Π. Π. Π’ΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΡΠΉ ΡΠ°ΠΊΡΠΎΡ p91/Stat1 ΠΊΠΎΠ½ΡΡΠΈΡΡΡΠΈΠ²Π½ΠΎ Π°ΠΊΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ ΠΈ Π»ΠΎΠΊΠ°Π»ΠΈΠ·ΡΠ΅ΡΡΡ Π² ΡΠ΄ΡΠ΅ ΡΠΌΠ±ΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΡ ΡΠΈΠ±ΡΠΎΠ±Π»Π°ΡΡΠΎΠ² ΠΊΡΡΡΡ, ΡΡΠ°Π½ΡΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π°ΠΌΠΈ E1A+Ha-Ras. ΠΠΎΠΊΠ». Π ΠΠ. 1996. 348: 261−264.
- Π Π΅ΡΠ΅ΡΠ½ΠΈΠΊΠΎΠ²Π° Π. Π€., ΠΠ΅ΡΡΠ΅ΡΠΎΠ² A.M., ΠΠΈΠΊΠΎΠ»ΡΡΠΊΠΈΠΉ Π. Π. Π€ΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ ΡΠΈΡΠΎΠ·ΠΈΠ½ΠΊΠΈΠ½Π°Π·Π½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΈΠ½ΡΠ΅ΡΠ½Π°Π»ΠΈΠ·ΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° ΠΠ€Π ΠΈ Π΅Π³ΠΎ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠ°. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 1990. 32: 140−147.
- Aniento F., Emans N., Griffiths G., Gruenberg J. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 1993. 123: 1373−1387.
- Aragane Y., Kulms D., Luger T.A., Schwarz T. Down-regulation of interferon gamma-activated STAT1 by UV light. Proc. Natl. Acad. Sci. USA. 1997. 94: 11 490−11 495.
- Aspenstrom P. The Rho GTPases have multiple effects on the actin cytoskeleton. Exp. Cell Res., 1999. 246: 20−25.
- BatzerA.G., Blaikie P., Nelson K., Schlessinger J., Margolis B. The phosphotyrosine interaction domain of She binds an LXNPXY motif on the epidermal growth factor receptor. Mol. Cell Biol. 1995.15: 4403−4409.
- Beguinot L., Lyall R.M., Willingham M.C., Pastan I. Down-regulation of the epidermal growth factor receptor in KB cells is due to receptor internalization and subsequent degradation in lysosomes. Proc Natl Acad Sci U S A. 1984. 81: 2384−2388.
- Bertics P.J., Gill G.N. Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor. J. Biol. Chem. 1985. 260: 14 642−14 647.
- Bevan A.P., Burgess J.W., Drake P.G., Shaver A., Bergeron J.J., Posner B.I. Selective activation of the rat hepatic endosomal insulin receptor kinase. Role for the endosome in insulin signaling. J. Biol. Chem. 1995. 270:10 784−10 791.
- Boonstra J., Rijken P., Humbel B., Cremers F., Verkleij A., van Bergen en Henegouwen P. The epidermal growth. Cell. Biol. Int. 1995.19: 413−430.
- Braun S., Raymond W.E., Racker E. Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases. J. Biol. Chem. 1984. 259: 2051−2054.
- Bucci C., Parton R.G., Mather I.H., Stunnenberg H., Simons K., Hoflack B., Zerial M. The small GTPase rab5 functions as a regulatory factor in the endocytic pathway. Cell. 1992. 70: 715−728.
- Burgess J.W., Wada I., Ling N., Khan M.N., Bergeron J.J., Posner B.I. Decrease in beta-subunit phosphotyrosine correlates with internalization and activation of the endosomal insulin receptor kinase. J. Biol. Chem. 1992. 267:10 077−10 086.
- Carpenter G. Receptor tyrosine kinase substrates: src homology domains and signal transduction. FASEB J. 1992. 6: 32 833 289.
- Carpenter G., King L., Cohen S. Epidermal growth factor stimulates phosphorylation in membrane preparations in vitro. Nature. 1978. 276: 409−410.
- Carpenter G., King L., Cohen S. Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. J. Biol. Chem. 1979. 254: 4884−4891.
- Carpenter G. Receptor for epidermal growth factor and other polypeptide mitogenes. Ann. Rev. Biochem. 1987. 56: 229−238.
- Carpentier J.-L., White M., Orci L., Kahn R. Direct visualization of EGF-R. J-Cell Biol. 1987. 105: 2751−2762.
- Chen W.S., Lazar C.S., Poenie M., Tsien R.Y., Cill G.N., Rosenfeld M.G. Requirement for intrinsic protein tyrosine kinase inthe immediate and late action of the EGF-receptor. Nature. 1987. 328: 820−823.
- Cheng H.C., Nishio H., Hatase 0., Ralph S., Wang J.H. A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases. J. Biol. Chem. 1992. 267: 9248−9256.
- Chin Y.E., Kitagawa M" Su W.C., You Z.H., Iwamoto Y" Fu X.Y. Cell growth arrest and induction of cyclin-dependent kinase inhibitor WAF1/CIP1 mediated by STAT1. Science. 1996. 272: 719 722.
- Chin Y.E., Kitagawa M. Kuida K. Flavell R.A., Fu X. Y. Activation of the STAT signaling pathway can cause expression of caspase 1 and apoptosis. Mol. Cell. Biol. 1997. 17: 5328−5337.
- Chung J., Uchida E., Grammer T.C., Blenis J. STAT3 serine phosphorylation by ERK-dependent and -independent pathways negatively modulates its tyrosine phosphorylation. Mol. Cell. Biol. 1997. 17:6508−6516.
- Cohen S. Isolation of a mouse submaxillary gland protein acceleration incisor eruption and eyelid opening in the newborn animal. J. Biol. Chem. 1962. 237: 1555−1562.
- Cohen S., Carpenter G., King L.J. EGF receptor-protein kinase interactions. J. Biol. Chem. 1980. 255: 4834−4843.
- Cohen S., Ushiro H., Stoscheck C., Chinkers M. A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles. J. Biol. Chem. 1982. 257: 1523−1531.
- Cohen S., Fava R.A. Internalization of functional EGF receptor kinase complexes in A431 cells. J. Biol. Chem. 1985. 260: 1 235 112 358.
- Darnell J.E. STATs and gene regulation. Science. 1997. 277:1630−1635.
- Darnell J.E. Phosphotyrosine signaling and the single cell: metazoan boundary. Proc.Natl. Acad. Sci. USA. 1997b. 94: 1 176 711 769.
- Davis R.J. Independent mechanism account for the regulation by PKC of the EGFR affinity and tyrosine kinase activity. J. Biol. Chem. 1988. 263: 9462−9469.
- Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucl. Acids Res. 1983.11.: 1475−1489.
- Ding A., Chen B., Fuortes M., Blum E. Association of mitogen-activated protein kinases with microtubules in mouse macrophages. J. Exp. Med. 1996. 183: 1899−1904.
- Downward J., Parker P., Waterfield M.D. Autophosphorylation sites on the epidermal growth factor receptor. Nature. 1984. 311: 483−485.
- Durbin J.E., Hackenmiller R., Celeste S.M., Levy D.E. Target disruption of the mouse Statl gene results in compromised innate immunity to viral disease. Cell. 1996. 84:443−450.
- Fruman D.A., Meyers R.E., Cantley L.C. Phosphoinositide kinases. Annu. Rev. Biochem. 1998. 67: 481−507.
- Fu X.Y., Schindler C., Improta T., Aebersold R., Darnell J.E. The proteins of ISGF-3, the interferon alpha-induced transcriptional activator, define a gene involved in signal transduction. Proc. Natl. Acad. Sci. USA. 1992. 89: 7840−7843.
- Fu X.-Y., Zhang J.J. Transcription factor p91 interact with the epidermal factor receptor and mediates activation of the c-fos gene promoter. Cell. 1993. 74: 1135−1145.
- Futter C., Felder S., Schlessinger J., Ullrich A., Hopkins C. Annexin 1 is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor. J. Cell Biol. 1993. 120: 77−83.
- Gatsios P., Terstegen L., Schliess F., Haussinger D., Kerr I.M., Heinrich P.C., Graeve L. Activation of the Janus kinase/signal transducer and activator of transcription pathway by osmotic shock. J. Biol. Chem. 1998. 273: 22 962−22 968.
- Glenney J.R., Chen J.W.S., Lazar C.S., Walton G.M., Zokas L.P., Rosenfeld M.G., Gill G.N. Ligand-induced endocytosis of the EGF receptor is blocked by mutant inactivation and by microinjection of anti-phosphotyrosine antibodies. Cell. 1988. 52: 675−684.
- Guglielmo G.M., Baass P.C., Ou W.J., Posner B.I., Bergeron J.J. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 1994. 13: 4269−4277.
- Grandis J.R., Drenning S.D., Chakraborty A., Zhou M.Y., Zeng Q., Pitt A.S., Tweardy D.J. Requirement of Stat3 but not Statl activation for epidermal growth factor receptor- mediated cell growth In vitro. J. Clin. Invest. 1998.102:1385−1392.
- Gruenberg J., Griffiths G., Howell K.E. Characterization of the early endosome and putative endocytic carrier vesicles in vivo andwith an assay of vesicle function in vitro. J. Cell Biol. 1989. 108: 1301−1316.
- Haigler H.T., Willingham M.C., Pastan I. Inhibitors of 1251-epidermal growth factor internalization. Biochem. Biophys. Res. Commun. 1980. 94: 630−637.
- Hall A. Rho GTPases and the actin cytoskeleton. Science. 1998. 279: 509−514.
- Haspel R.L., Salditt Georgieff M., Darnell J.E., Jr. The rapid inactivation of nuclear tyrosine phosphorylated Statl depends upon a protein tyrosine phosphatase. EMBO J. 1996. 15: 6262−6268.
- Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 1998. 279: 519−526.
- Horvai A.E., Xu L., Korzus E., Brard G., Kalafus D., Mullen T.M. Rose D.W., Rosenfeld M.G., Glass C.K. Nuclear integration of JAK/STAT and Ras/AP-1 signaling by CBP and p300. Proc. Natl. Acad. Sci. USA. 1997. 94: 1074−1079.
- Jans D.A., Briggs L.J., Gustin S.E., Jans P., Ford S., Young I.G. The cytokine interleukin-5 (IL-5) effects cotransport of its receptor subunits to the nucleus in vitro. FEBS Lett. 1997. 410: 368−372.
- Johnson H.M., Torres B.A., Green M.M., Szente B.E., Siler K.I., Larkin J., Subramaniam P. S. Hypothesis: ligand/receptor-assisted nuclear translocation of STATs. Proc. Soc. Exp. Biol. Med. 1998. 218: 149−155.
- Kashles O., Szapary D., Bellot F., Ullrich A., Schlessinger J., Schmidt A. Ligand-induced stimulation of EGF-receptor mutants with altered trans-membrane region. Proc. Nat. Acad. Sci. USA. 1988. 85: 9567−9571.
- Kay D.G., Lai W.H., Uchihashi M., Khan M.N., Posner B.I., Bergeron J.J.M. EGF receptor kinase translocation and activation in vivo. J. Biol. Chem. 1986. 261: 8473−8480.
- Keenan C- Kelleher D Protein kinase C and the cytoskeleton. Cell. Signal. 1998. 10: 225−232.
- Khan M.N., Baquiran G., Brule C., Burgess J., Foster B., Bergeron. J.J., Posner B.I. Internalization and activation of the rat liver insulin receptor kinase in vivo. J. Biol. Chem. 1989. 264: 1 293 112 940.
- Klemm J.D., Schreiber S.L., Crabtree G.R. Dimerization as a regulatory mechanism in signal transduction. Annu. Rev. Immunol. 1998 16:569−592.
- Koch C.A., Anderson D. Moran M.F., Ellis C. Pawson T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. 1991. 252: 668−674.
- Margolis Π., Rhee S.G., Felder S., Mervic M., Lyall R., Levitzki A., Ullrich A., Zilberstein A., Schlessinger J. EGF induces tyrosine phosphorylation of phospholipase C-ll: a potential mechanism for EGF receptor signaling. Cell. 1989. 57:1101−1107.
- Mayo K.H. Epidermal growth factor from the mouse. Biochemistry. 1995. 24: 3783−3794.
- McCormick. How receptors turn Ras on. Nature. 1993. 363: 1516.
- Melamed I., Franklin R.A., Gelfand E.W. Microfilament assembly is- required for anti-IgM dependent ΠΠΠ Π and p90rsk activation in human Π lymphocytes. Biochem. Biophys. Res. Commun. 1995. 209: 1102−1110.
- Mermall V., Post P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 1998. 279: 527−533.
- Mohammadi M., Honegger A., Sorokin A., Ullrich A., Schlessinger J., Hurwitz D.R. Aggregation-induced activation of the epidermal growth factor receptor protein tyrosine kinase. Biochemistry. 1993. 32: 8742−8748.
- Nesterov A., Reshetnikova G., Vinogradova N., Nikolsky. Funktional state of the EGF receptor complexes duting their internalization in A431 cells. Mol. Cell. Biol. 1990. 10: 5011−5014. .
- Nesterov A., Lysan S., Vdovina I., Nikolsky N., Fujita D.J. Phosphorylation of the epidermal growth factor receptor during internalization in A-431 cells. Arch. Biochem. Biophys. 1994. 313: 351−359.
- Nigg E.A. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature. 1997. 386: 779−787.
- Pastan I.H., Willingham M.C. Receptor-mediated endocytosis of hormones in cultured cells. Ann. Rev. Phisiol. 1981. 43: 239−250.
- Pawson T., Schlessinger J. SH2 and SH3 domains. Current Biol. 1993. 3: 434−441.
- Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 1977. 83: 346−356.
- Pfeffer L.M., Mullersman J.E., Pfeffer S.R., Murti A., Shi W.(Yang C.H. STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor. Science. 1997. 276: 1418−1420.
- Riese D.J., Stern D.F. Specificity within the EGF family/ErbB receptor family signaling network. Bioessays. 1998. 20: 41−48.
- Ruff-Jamison S., Chen K., Cohen S. Induction by EGF and interferon-g of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science. 1993. 261:1733−1736.
- Sadowski H.B., Gilman M.Z. Cell-free activation of a DNA-binding protein by epidermal growth factor. Nature. 1993. 362: 79−83.
- Sadowski H.B., Shuai K., Darnell J.E., Gilman M.Z. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science. 1993. 261:1739−1744.
- Savage C.R., Cohen S. Epidermal growth factor and a new derivative: rapid isolation procedures and biological and chemical characterization. J. Biol. Chem. 1972. 247: 7609−7611.
- Savage C.R., Cohen S. Proliferation of corneal epithelium induced by epidermal growth factor. Exp. Eye Res. 1973. 15: 361 366.
- Schindler C., Shuai K., Prezioso V.R., Darnell J.E. Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor. Science. 1992. 257: 809−813.
- Schindler C., Fu X.Y., Improta T.(Aebersold R., Darnell J.E. Proteins of transcription factor ISGF-3: one gene encodes the 91-and 84-kDa ISGF-3 proteins that are activated by interferon alpha. Proc. Natl. Acad. Sci. USA. 1992b. 89: 7836−7839.
- Schlessinger J., Ullrich A. Growth factor signaling by receptor tyrosine kinases. Neuron. 1992. 9: 383−391.
- Schmalz D., Hucho F., Buchner K. Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal. J. Cell Sci. 1998.111:1823−1830.
- Sekimoto T., Imamoto N., Nakajima K., Hirano T., Yoneda Y. Extracellular signal-dependent nuclear import of Statl is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 1997. 16: 7067−7077.
- Shuai K., Shindler C., Prezioso V.R., Darnell J.E. Activation of transcription by IFN-g: tyrosine phosphorylation of a 91-kD DNA binding protein. Science. 1992. 258: 1808−1812.
- Shuai K., Stark G.R., Kerr I.M., Darnell J.E. A single phosphotyrosine residue of stat91 required for gene activation by interferon-g. Science. 1993. 261:1744−1746.
- Shuai K., Horvath C.M., Tsai Huang L.H., Qureshi S.A., Cowburn D., Darnell J.E. Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell. 1994. 76: 821−828.
- Silvennoinen O., Schindler C., Schlessinger J., Levy D.E. Ras-independent growth factor signaling by transcription factor tyrosine phosphorylation. Science. 1993. 261:1736−1739.
- Singer W.D., Brown H.A., Sternweis P.C. Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D. Annu. Rev. Biochem. 1997. 66: 475−509.
- Smith H.M., Raikhel N.V. Nuclear localization signal receptor importin alpha associates with cytoskeleton. Plant Cell. 1998. 10: 1791−1799.
- Soderquist A.M., Carpenter G. Glycosylation of the epidermal growth factor receptor in A-431 cells. The contribution of carbohydrate to receptor function. J. Biol. Chem. 1984. 259: 1 258 612 594.
- Sorkin A.D. Teslenko L.V. Nikolsky N.N. The endocytosis of epidermal growth factor in A431 cells: a pH of microenvironment and the dynamics of receptor complex dissociation. Exp. Cell Res. 1988. 175: 192−205.
- Sorkin A., Carpenter G. Dimerization of internalized EGF receptor. J. Biol. Chem. 1991. 266: 23 453−23 460.
- Sorokin A., Lemmon G., Ullrich A., Schlessinger J. Stabilization of an active dimeric form of EGFreceptor by introduction of an interreceptor disulfide bond. J. Biol. Chem. 1994. 269: 9752−9759.
- Stancato L.F., Yu C.R., Petricoin E.F., 3rd, Larner A.C. Activation of Raf-1 by interferon gamma and oncostatin M requires expression of the Statl transcription factor. J. Biol. Chem. 1998. 273: 18 701−18 704.
- Ullrich A., Schlessinger J. Signal transduction by receptor with tyrosine kinase activity. Cell. 1990. 61: 287−307.
- Vieira A.V., Lamaze C., Schmid S.L., Control of EGF receptor signaling by clathrin-mediated endocytosis. Science. 1996. 274: 2086−2089.
- Wada I., Lai W.H., Posner B.I., Bergeron J.J. Association of the tyrosine phosphorylated EGF receptor with a 55-kD tyrosine phosphorylated protein at the cell surface and in endosomes. J. Cell Biol. 1992. 116: 321−330.
- Warren G. Trawling for receptors. Nature. 1990. 346: 318−319.
- Wen Z., Zhong Z., Darnell J.E., Jr. Maximal activation of transcription by Statl and Stat3 requires both tyrosine and serine phosphorylation. Cell. 1995. 82: 241−250.
- Wiesmuller L., Wittinghofer F. Signal transduction pathways involving Ras. Cell. Signal. 1994. 6: 247−267.
- Wiley H.S., Cunningham D.D. The endocytic rate constant. A cellular parameter for quantitative receptor-mediated endocytosis. J. Biol. Chem. 1982. 257: 4222−4229.
- Xu X., Fu X.Y., Plate J., Chong A.S. IFN-gamma induces cell growth inhibition by Fas-mediated apoptosis: requirement of STAT1 protein for up-regulation of Fas and FasL expression. Cancer Res. 1998. 58: 2832−2837.
- Xue L., Lucocq J. ERK2 signalling from internalized epidermal growth factor receptor in broken A431 cells. Cell. Signal. 1998. 10: 339−348.
- Zhang J.J., Vinkemeier U., Gu W., Chakravarti D., Horvath C.M., Darnell J.E., Jr. Two contact regions between Statl and107
- CBP/p300 in interferon gamma signaling. Proc. Natl. Acad. Sci. USA. 1996. 93: 15 092−15 096.
- Zheng Z.M., Specter S. Delta-9-tetrahydrocannabinol: an inhibitor of STAT1 alpha protein tyrosine phosphorylation. Biochem. Pharmacol. 1996. 51: 967−973.
- Zhu X., Wen Z., Xu L.Z., Darnell J.E., Jr. Statl serine phosphorylation occurs independently of tyrosine phosphorylation and requires an activated Jak2 kinase. Mol. Cell. Biol. 1997. 17: 6618−6623.