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Volumn 325, Issue 1-2, 2010, Pages 143-149

Prolactin-induced Jak2 phosphorylation of RUSH: A key element in Jak/RUSH signaling

Author keywords

Actin; HLTF; HRE H9 cells (rabbit endometrium); Jak2; Nucleolin; Prolactin

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; FIBRILLARIN; JANUS KINASE 2; JANUS KINASE 2 INHIBITOR; NUCLEAR PROTEIN; NUCLEOLIN; PROGESTERONE; PROLACTIN; PROTEIN RUSH; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 77954383159     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2010.05.010     Document Type: Article
Times cited : (12)

References (41)
  • 5
    • 77953476421 scopus 로고    scopus 로고
    • Impact of prolactin receptor isoforms on reproduction
    • Binart N., Bachelot A., Bouilly J. Impact of prolactin receptor isoforms on reproduction. Trends Endocrinol Metab. 2010, 21:362-368.
    • (2010) Trends Endocrinol Metab. , vol.21 , pp. 362-368
    • Binart, N.1    Bachelot, A.2    Bouilly, J.3
  • 7
    • 0024268286 scopus 로고
    • Servomechanism of prolactin and progesterone in regulating uterine gene expression
    • Chilton B.S., Mani S.K., Bullock D.W. Servomechanism of prolactin and progesterone in regulating uterine gene expression. Mol. Endocrinol. 1988, 2:1169-1175.
    • (1988) Mol. Endocrinol. , vol.2 , pp. 1169-1175
    • Chilton, B.S.1    Mani, S.K.2    Bullock, D.W.3
  • 8
    • 0032483043 scopus 로고    scopus 로고
    • Rabbit β-globin is extended beyond its UGA stop codon by multiple suppressions and translational reading gaps
    • Chittum H.S., Lane W.S., Carlson B.A., Roller P.P., Lung F.T., Lee B.J., Hatfield D.L. Rabbit β-globin is extended beyond its UGA stop codon by multiple suppressions and translational reading gaps. Biochemistry 1998, 37:10866-10870.
    • (1998) Biochemistry , vol.37 , pp. 10866-10870
    • Chittum, H.S.1    Lane, W.S.2    Carlson, B.A.3    Roller, P.P.4    Lung, F.T.5    Lee, B.J.6    Hatfield, D.L.7
  • 10
    • 84944661914 scopus 로고
    • Rank transformation as a bridge between parametric and nonparametric statistics
    • Conover W.J., Iman R.L. Rank transformation as a bridge between parametric and nonparametric statistics. Am. Stat. 1981, 35:124-129.
    • (1981) Am. Stat. , vol.35 , pp. 124-129
    • Conover, W.J.1    Iman, R.L.2
  • 13
    • 61849119563 scopus 로고    scopus 로고
    • Nucleolar targeting: the hub of the matter
    • Emmott E., Hiscox J.A. Nucleolar targeting: the hub of the matter. EMBO Rep. 2009, 10:231-238.
    • (2009) EMBO Rep. , vol.10 , pp. 231-238
    • Emmott, E.1    Hiscox, J.A.2
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormick A.L., Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormick, A.L.2    Yates, J.R.3
  • 15
    • 44449139885 scopus 로고    scopus 로고
    • Chromatin remodeling and actin organization
    • Farrants A.K. Chromatin remodeling and actin organization. FEBS Lett. 2008, 582:2041-2050.
    • (2008) FEBS Lett. , vol.582 , pp. 2041-2050
    • Farrants, A.K.1
  • 16
    • 0030476454 scopus 로고    scopus 로고
    • Cloning, characterization and steroid-dependent posttranscriptional processing of RUSH-1α and β, two uteroglobin promoter-binding proteins
    • Hayward-Lester A., Hewetson A., Beale E.G., Oefner P.J., Doris P.A., Chilton B.S. Cloning, characterization and steroid-dependent posttranscriptional processing of RUSH-1α and β, two uteroglobin promoter-binding proteins. Mol. Endocrinol. 1996, 10:1335-1349.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1335-1349
    • Hayward-Lester, A.1    Hewetson, A.2    Beale, E.G.3    Oefner, P.J.4    Doris, P.A.5    Chilton, B.S.6
  • 17
    • 41149149301 scopus 로고    scopus 로고
    • Interpretation of cytokine signaling through the transcription factors STAT5A and STAT5B
    • Hennighausen L., Robinson G.W. Interpretation of cytokine signaling through the transcription factors STAT5A and STAT5B. Genes Dev. 2008, 22:711-721.
    • (2008) Genes Dev. , vol.22 , pp. 711-721
    • Hennighausen, L.1    Robinson, G.W.2
  • 18
    • 0036716913 scopus 로고    scopus 로고
    • Identification of the RUSH consensus-binding site by cyclic amplification and selection of targets: demonstration that RUSH mediates the ability of prolactin to augment progesterone-dependent gene expression
    • Hewetson A., Hendrix E.C., Mansharamani M., Lee V.H., Chilton B.S. Identification of the RUSH consensus-binding site by cyclic amplification and selection of targets: demonstration that RUSH mediates the ability of prolactin to augment progesterone-dependent gene expression. Mol. Endocrinol. 2002, 16:2101-2112.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2101-2112
    • Hewetson, A.1    Hendrix, E.C.2    Mansharamani, M.3    Lee, V.H.4    Chilton, B.S.5
  • 19
    • 0141994713 scopus 로고    scopus 로고
    • An Sp1-NF-Y/Progesterone receptor DNA binding-dependent mechanism regulates progesterone-induced transcriptional activation of the rabbit RUSH/SMARCA3 gene
    • Hewetson A., Chilton B.S. An Sp1-NF-Y/Progesterone receptor DNA binding-dependent mechanism regulates progesterone-induced transcriptional activation of the rabbit RUSH/SMARCA3 gene. J. Biol. Chem. 2003, 278:40177-40185.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40177-40185
    • Hewetson, A.1    Chilton, B.S.2
  • 20
    • 9744241674 scopus 로고    scopus 로고
    • Prolactin signals through RUSH/SMARCA3 in the absence of a physical association with Stat5a
    • Hewetson A., Moore S.L., Chilton B.S. Prolactin signals through RUSH/SMARCA3 in the absence of a physical association with Stat5a. Biol. Reprod. 2004, 71:1907-1912.
    • (2004) Biol. Reprod. , vol.71 , pp. 1907-1912
    • Hewetson, A.1    Moore, S.L.2    Chilton, B.S.3
  • 22
    • 41649111599 scopus 로고    scopus 로고
    • Progesterone-dependent DNA looping between RUSH/SMARCA3 and Egr-1 mediates repression by c-Rel
    • Hewetson A., Chilton B.S. Progesterone-dependent DNA looping between RUSH/SMARCA3 and Egr-1 mediates repression by c-Rel. Mol. Endocrinol. 2008, 22:813-822.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 813-822
    • Hewetson, A.1    Chilton, B.S.2
  • 23
    • 33645711927 scopus 로고    scopus 로고
    • The HIRAN domain and recruitment of chromatin remodeling and repair activities to damaged DNA
    • Iyer L.M., Babu M.M., Aravind L. The HIRAN domain and recruitment of chromatin remodeling and repair activities to damaged DNA. Cell Cycle 2006, 5:775-782.
    • (2006) Cell Cycle , vol.5 , pp. 775-782
    • Iyer, L.M.1    Babu, M.M.2    Aravind, L.3
  • 24
    • 0027477720 scopus 로고
    • Prolactin augments progesterone-dependent uteroglobin gene expression by modulating promoter-binding proteins
    • Kleis-SanFrancisco S., Hewetson A., Chilton B.S. Prolactin augments progesterone-dependent uteroglobin gene expression by modulating promoter-binding proteins. Mol. Endocrinol. 1993, 7:214-223.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 214-223
    • Kleis-SanFrancisco, S.1    Hewetson, A.2    Chilton, B.S.3
  • 25
    • 0024370753 scopus 로고
    • Characterization of a temperature-sensitive β-endorphin-secreting transformed endometrial cell line
    • Li W.I., Chen C.L., Chou J.Y. Characterization of a temperature-sensitive β-endorphin-secreting transformed endometrial cell line. Endocrinology 1989, 125:2862-2867.
    • (1989) Endocrinology , vol.125 , pp. 2862-2867
    • Li, W.I.1    Chen, C.L.2    Chou, J.Y.3
  • 26
    • 54049101441 scopus 로고    scopus 로고
    • Canonical and non-canonical JAK-STAT signaling
    • Li W.X. Canonical and non-canonical JAK-STAT signaling. Trends Cell Biol. 2008, 18:545-551.
    • (2008) Trends Cell Biol. , vol.18 , pp. 545-551
    • Li, W.X.1
  • 27
    • 0029962298 scopus 로고    scopus 로고
    • C23 interacts with B23, a putative nucleolar-localization-signal-binding protein
    • Li Y.P., Busch R.K., Valdez B.C., Busch H. C23 interacts with B23, a putative nucleolar-localization-signal-binding protein. Eur. J. Biochem. 1996, 237:153-158.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 153-158
    • Li, Y.P.1    Busch, R.K.2    Valdez, B.C.3    Busch, H.4
  • 29
    • 58049173935 scopus 로고    scopus 로고
    • Chapter 3. Transcriptional control of gene expression by actin and myosin
    • Louvet E., Percipalle P. Chapter 3. Transcriptional control of gene expression by actin and myosin. Int. Rev. Cell Mol. Biol. 2009, 272:107-147.
    • (2009) Int. Rev. Cell Mol. Biol. , vol.272 , pp. 107-147
    • Louvet, E.1    Percipalle, P.2
  • 30
    • 0035793608 scopus 로고    scopus 로고
    • Cloning and characterization of an atypical type IV P-type ATPase that binds to the RING motif of RUSH transcription factors
    • Mansharamani M., Hewetson A., Chilton B.S. Cloning and characterization of an atypical type IV P-type ATPase that binds to the RING motif of RUSH transcription factors. J. Biol. Chem. 2001, 276:3641-3649.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3641-3649
    • Mansharamani, M.1    Hewetson, A.2    Chilton, B.S.3
  • 31
    • 33846681638 scopus 로고    scopus 로고
    • Nucleolin: a multiFACeTed protein
    • Mongelard F., Bouvet P. Nucleolin: a multiFACeTed protein. Trends Cell Biol. 2007, 17:80-86.
    • (2007) Trends Cell Biol. , vol.17 , pp. 80-86
    • Mongelard, F.1    Bouvet, P.2
  • 32
    • 37349074529 scopus 로고    scopus 로고
    • Uteroglobin: a steroid-inducible immunomodulatory protein that founded the secretoglobin superfamily
    • Mukherjee A.B., Zhang Z., Chilton B.S. Uteroglobin: a steroid-inducible immunomodulatory protein that founded the secretoglobin superfamily. Endocr. Rev. 2007, 28:707-725.
    • (2007) Endocr. Rev. , vol.28 , pp. 707-725
    • Mukherjee, A.B.1    Zhang, Z.2    Chilton, B.S.3
  • 33
    • 77749341438 scopus 로고    scopus 로고
    • Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity
    • Nagy V., Dikic I. Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity. Biol Chem. 2010, 391:163-169.
    • (2010) Biol Chem. , vol.391 , pp. 163-169
    • Nagy, V.1    Dikic, I.2
  • 34
    • 33746531672 scopus 로고    scopus 로고
    • Nuclear Jak2 and transcription factor NF1-C2: a novel mechanism of prolactin signaling in mammary epithelial cells
    • Nilsson J., Bjursell G., Kannius-Janson M. Nuclear Jak2 and transcription factor NF1-C2: a novel mechanism of prolactin signaling in mammary epithelial cells. Mol. Cell. Biol. 2006, 26:5663-5674.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5663-5674
    • Nilsson, J.1    Bjursell, G.2    Kannius-Janson, M.3
  • 35
    • 44449099142 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling enzymes: two heads are not better, just different
    • Racki L.R., Narlikar G.J. ATP-dependent chromatin remodeling enzymes: two heads are not better, just different. Curr. Opin. Genet. Dev. 2008, 18:137-144.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 137-144
    • Racki, L.R.1    Narlikar, G.J.2
  • 36
    • 70350494529 scopus 로고    scopus 로고
    • JAK2 gets histone H3 rolling
    • Sattler M., Griffin J.D. JAK2 gets histone H3 rolling. Cancer Cell 2009, 16:365-366.
    • (2009) Cancer Cell , vol.16 , pp. 365-366
    • Sattler, M.1    Griffin, J.D.2
  • 38
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitination-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • Ungureanu D., Saharinen P., Junttila I., Hilton D.J., Silvennoinen O. Regulation of Jak2 through the ubiquitination-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol. Cell. Biol. 2002, 22:3316-3326.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3316-3326
    • Ungureanu, D.1    Saharinen, P.2    Junttila, I.3    Hilton, D.J.4    Silvennoinen, O.5
  • 39
    • 0030983549 scopus 로고    scopus 로고
    • Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation
    • Yu C.L., Burakoff S.J. Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation. J. Biol. Chem. 1997, 272:14017-14020.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14017-14020
    • Yu, C.L.1    Burakoff, S.J.2
  • 40
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 2005, 4:1240-1250.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 41
    • 65349161753 scopus 로고    scopus 로고
    • Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression
    • Zheng B., Han M., Bernier M., Wen J.K. Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression. FEBS J. 2009, 276:2669-2685.
    • (2009) FEBS J. , vol.276 , pp. 2669-2685
    • Zheng, B.1    Han, M.2    Bernier, M.3    Wen, J.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.