메뉴 건너뛰기




Volumn 439, Issue , 2008, Pages 171-180

Rac and Nuclear Translocation of Signal Transducers and Activators of Transcription Factors

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIGITONIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; KARYOPHERIN ALPHA; KARYOPHERIN BETA; NUCLEAR PROTEIN; RAC PROTEIN; RAC1 PROTEIN; RECOMBINANT PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; STAT PROTEIN; TRANSCRIPTION FACTOR; MGCRACGAP; STAT5 PROTEIN;

EID: 45549100578     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)00413-2     Document Type: Review
Times cited : (5)

References (26)
  • 1
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam S.A., Marr R.S., and Gerace L. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111 (1990) 807-816
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 2
    • 0027024350 scopus 로고
    • Nuclear protein import using digitonin-permeabilized cells
    • Adam S.A., Marr R.S., and Gerace L. Nuclear protein import using digitonin-permeabilized cells. Methods Enzymol. 219 (1992) 97-110
    • (1992) Methods Enzymol. , vol.219 , pp. 97-110
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 3
    • 0034981517 scopus 로고    scopus 로고
    • STAT proteins: Signal transducers and activators of transcription
    • Bromberg J., and Chen X.M. STAT proteins: Signal transducers and activators of transcription. Methods Enzymol. 333 (2001) 138-151
    • (2001) Methods Enzymol. , vol.333 , pp. 138-151
    • Bromberg, J.1    Chen, X.M.2
  • 4
    • 0029693897 scopus 로고    scopus 로고
    • The JAK-STAT pathway: Summary of initial studies and recent advances
    • Darnell Jr. J.E. The JAK-STAT pathway: Summary of initial studies and recent advances. Recent Prog. Horm. Res. 51 (1996) 391-403
    • (1996) Recent Prog. Horm. Res. , vol.51 , pp. 391-403
    • Darnell Jr., J.E.1
  • 5
    • 0036782706 scopus 로고    scopus 로고
    • Transcription factors as targets for cancer therapy
    • Darnell Jr. J.E. Transcription factors as targets for cancer therapy. Nat. Rev. Cancer 2 (2002) 740-749
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 740-749
    • Darnell Jr., J.E.1
  • 6
    • 0030851775 scopus 로고    scopus 로고
    • The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IkappaBalpha and stimulates its degradation in vitro
    • Ghoda L., Lin X., and Greene W.C. The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IkappaBalpha and stimulates its degradation in vitro. J. Biol. Chem. 272 (1997) 21281-21288
    • (1997) J. Biol. Chem. , vol.272 , pp. 21281-21288
    • Ghoda, L.1    Lin, X.2    Greene, W.C.3
  • 7
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D., and Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15 (1999) 607-660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 8
    • 0032584671 scopus 로고    scopus 로고
    • Phosphorylation at the nuclear localization signal of Ca2+/calmodulin-dependent protein kinase II blocks its nuclear targeting
    • Heist E.K., Srinivasan M., and Schulman H. Phosphorylation at the nuclear localization signal of Ca2+/calmodulin-dependent protein kinase II blocks its nuclear targeting. J. Biol. Chem. 273 (1998) 19763-19771
    • (1998) J. Biol. Chem. , vol.273 , pp. 19763-19771
    • Heist, E.K.1    Srinivasan, M.2    Schulman, H.3
  • 9
    • 0035937180 scopus 로고    scopus 로고
    • MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody
    • Hirose K., Kawashima T., Iwamoto I., Nosaka T., and Kitamura T. MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody. J. Biol. Chem. 276 (2001) 5821-5828
    • (2001) J. Biol. Chem. , vol.276 , pp. 5821-5828
    • Hirose, K.1    Kawashima, T.2    Iwamoto, I.3    Nosaka, T.4    Kitamura, T.5
  • 13
    • 20444400857 scopus 로고    scopus 로고
    • STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-alpha3
    • Liu L., McBride K.M., and Reich N.C. STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-alpha3. Proc. Natl. Acad. Sci. USA 102 (2005) 8150-8155
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8150-8155
    • Liu, L.1    McBride, K.M.2    Reich, N.C.3
  • 14
    • 33646365075 scopus 로고    scopus 로고
    • Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements
    • Ma J., and Cao X. Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements. Cell Signal. 18 (2006) 1117-1126
    • (2006) Cell Signal. , vol.18 , pp. 1117-1126
    • Ma, J.1    Cao, X.2
  • 15
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj I., and Englmeier L. Nucleocytoplasmic transport: The soluble phase. Annu. Rev. Biochem. 67 (1998) 265-306
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.1    Englmeier, L.2
  • 16
    • 0034658668 scopus 로고    scopus 로고
    • Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast
    • Mattison C.P., and Ota I.M. Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast. Genes Dev. 14 (2000) 1229-1235
    • (2000) Genes Dev. , vol.14 , pp. 1229-1235
    • Mattison, C.P.1    Ota, I.M.2
  • 17
    • 0037007207 scopus 로고    scopus 로고
    • Regulated nuclear import of the STAT1 transcription factor by direct binding of importin-α
    • McBride K.M., Banninger G., McDonald C., and Reich N.C. Regulated nuclear import of the STAT1 transcription factor by direct binding of importin-α. EMBO J. 21 (2002) 1754-1763
    • (2002) EMBO J. , vol.21 , pp. 1754-1763
    • McBride, K.M.1    Banninger, G.2    McDonald, C.3    Reich, N.C.4
  • 18
    • 0029133520 scopus 로고
    • Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor
    • Quelle F.W., Thierfelder W., Witthuhn B.A., Tang B., Cohen S., and Ihle J.N. Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor. J. Biol. Chem. 270 (1995) 20775-20780
    • (1995) J. Biol. Chem. , vol.270 , pp. 20775-20780
    • Quelle, F.W.1    Thierfelder, W.2    Witthuhn, B.A.3    Tang, B.4    Cohen, S.5    Ihle, J.N.6
  • 19
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • Saharinen P., Takaluoma K., and Silvennoinen O. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20 (2000) 3387-3395
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 20
    • 0030670639 scopus 로고    scopus 로고
    • Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1
    • Sekimoto T., Imamoto N., Nakajima K., Hirano T., and Yoneda Y. Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 16 (1997) 7067-7077
    • (1997) EMBO J. , vol.16 , pp. 7067-7077
    • Sekimoto, T.1    Imamoto, N.2    Nakajima, K.3    Hirano, T.4    Yoneda, Y.5
  • 21
    • 0029009479 scopus 로고
    • The cell cycle-dependent nuclear import of v-Jun is regulated by phosphorylation of a serine adjacent to the nuclear localization signal
    • Tagawa T., Kuroki T., Vogt P.K., and Chida K. The cell cycle-dependent nuclear import of v-Jun is regulated by phosphorylation of a serine adjacent to the nuclear localization signal. J. Cell Biol. 130 (1995) 255-263
    • (1995) J. Cell Biol. , vol.130 , pp. 255-263
    • Tagawa, T.1    Kuroki, T.2    Vogt, P.K.3    Chida, K.4
  • 23
    • 0029903770 scopus 로고    scopus 로고
    • DNA binding of in vitro activated Stat1 alpha, Stat1 beta and truncated Stat1: Interaction between NH2-terminal domains stabilizes binding of two dimers to tandem DNA sites
    • Vinkemeier U., Cohen S.L., Moarefi I., Chait B.T., Kuriyan J., and Darnell Jr. J.E. DNA binding of in vitro activated Stat1 alpha, Stat1 beta and truncated Stat1: Interaction between NH2-terminal domains stabilizes binding of two dimers to tandem DNA sites. EMBO J. 15 (1996) 5616-5626
    • (1996) EMBO J. , vol.15 , pp. 5616-5626
    • Vinkemeier, U.1    Cohen, S.L.2    Moarefi, I.3    Chait, B.T.4    Kuriyan, J.5    Darnell Jr., J.E.6
  • 24
    • 0032772369 scopus 로고    scopus 로고
    • Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha
    • Weil R., Sirma H., Giannini C., Kremsdorf D., Bessia C., Dargemont C., Brechot C., and Israel A. Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha. Mol. Cell. Biol. 19 (1999) 6345-6354
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6345-6354
    • Weil, R.1    Sirma, H.2    Giannini, C.3    Kremsdorf, D.4    Bessia, C.5    Dargemont, C.6    Brechot, C.7    Israel, A.8
  • 25
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S., Marrero L., and Jones F.E. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J. Cell Biol. 167 (2004) 469-478
    • (2004) J. Cell Biol. , vol.167 , pp. 469-478
    • Williams, C.C.1    Allison, J.G.2    Vidal, G.A.3    Burow, M.E.4    Beckman, B.S.5    Marrero, L.6    Jones, F.E.7
  • 26
    • 16944365287 scopus 로고    scopus 로고
    • Internal tandem duplication of the FLT3 gene is preferentially seen in acute myeloid leukemia and myelodysplastic syndrome among various hematological malignancies: A study on a large series of patients and cell lines
    • Yokota S., Kiyoi H., Nakao M., Iwai T., Misawa S., Okuda T., Sonoda Y., Abe T., Kahsima K., Matsuo Y., and Naoe T. Internal tandem duplication of the FLT3 gene is preferentially seen in acute myeloid leukemia and myelodysplastic syndrome among various hematological malignancies: A study on a large series of patients and cell lines. Leukemia 11 (1997) 1605-1609
    • (1997) Leukemia , vol.11 , pp. 1605-1609
    • Yokota, S.1    Kiyoi, H.2    Nakao, M.3    Iwai, T.4    Misawa, S.5    Okuda, T.6    Sonoda, Y.7    Abe, T.8    Kahsima, K.9    Matsuo, Y.10    Naoe, T.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.