메뉴 건너뛰기




Volumn 8, Issue 10, 2007, Pages 914-919

The inner nuclear envelope as a transcription factor resting place

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; LAMININ; TRANSCRIPTION FACTOR;

EID: 34848872591     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7401075     Document Type: Review
Times cited : (129)

References (40)
  • 1
    • 7644241534 scopus 로고    scopus 로고
    • Amino acid signaling in yeast: Casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor
    • Abdel-Sater F, El Bakkoury M, Urrestarazu A, Vissers S, Andre B (2004) Amino acid signaling in yeast: Casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor. Mol Cell Biol 24: 9771-9785
    • (2004) Mol Cell Biol , vol.24 , pp. 9771-9785
    • Abdel-Sater, F.1    El Bakkoury, M.2    Urrestarazu, A.3    Vissers, S.4    Andre, B.5
  • 2
    • 34250777112 scopus 로고    scopus 로고
    • The nuclear envelope and transcriptional control
    • Akhtar A, Gasser SM (2007) The nuclear envelope and transcriptional control. Nat Rev Genet 8: 507-517
    • (2007) Nat Rev Genet , vol.8 , pp. 507-517
    • Akhtar, A.1    Gasser, S.M.2
  • 3
    • 0037115602 scopus 로고    scopus 로고
    • Receptor-mediated endoproteolytic activation of two transcription factors in yeast
    • Andreasson C, Ljungdahl PO (2002) Receptor-mediated endoproteolytic activation of two transcription factors in yeast. Genes Dev 16 3158-3172
    • (2002) Genes Dev , vol.16 , pp. 3158-3172
    • Andreasson, C.1    Ljungdahl, P.O.2
  • 4
    • 33745165630 scopus 로고    scopus 로고
    • Regulation of transcription factor latency by receptor-activated proteolysis
    • Andreasson C, Heessen S, Ljungdahl PO (2006) Regulation of transcription factor latency by receptor-activated proteolysis. Genes Dev 20 1563-1568
    • (2006) Genes Dev , vol.20 , pp. 1563-1568
    • Andreasson, C.1    Heessen, S.2    Ljungdahl, P.O.3
  • 5
    • 33847408864 scopus 로고    scopus 로고
    • What MAN1 does to the Smads. TGFβ/BMP signaling and the nuclear envelope
    • Bengtsson L (2007) What MAN1 does to the Smads. TGFβ/BMP signaling and the nuclear envelope. FEBS J 274: 1374-1362
    • (2007) FEBS J , vol.274 , pp. 1374-1362
    • Bengtsson, L.1
  • 6
    • 33747435504 scopus 로고    scopus 로고
    • Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors
    • Boban M, Zargari A, Andreasson C, Heessen S, Thyberg J, Ljungdahl PO (2006) Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors. J Cell Biol 173: 695-707
    • (2006) J Cell Biol , vol.173 , pp. 695-707
    • Boban, M.1    Zargari, A.2    Andreasson, C.3    Heessen, S.4    Thyberg, J.5    Ljungdahl, P.O.6
  • 7
    • 20444449733 scopus 로고    scopus 로고
    • Altered pre-lamin A processing is a common mechanism leading to lipodystrophy
    • Capanni C et al (2005) Altered pre-lamin A processing is a common mechanism leading to lipodystrophy. Hum Mol Genet 14: 1489-1502
    • (2005) Hum Mol Genet , vol.14 , pp. 1489-1502
    • Capanni, C.1
  • 8
    • 34248154716 scopus 로고    scopus 로고
    • The nuclear envelope protein MAN1 regulates TGFβ signaling and vasculogenesis in the embryonic yolk sac
    • Cohen TV, Kosti O, Stewart CL (2007) The nuclear envelope protein MAN1 regulates TGFβ signaling and vasculogenesis in the embryonic yolk sac. Development 134: 1385-1395
    • (2007) Development , vol.134 , pp. 1385-1395
    • Cohen, T.V.1    Kosti, O.2    Stewart, C.L.3
  • 9
    • 0034651810 scopus 로고    scopus 로고
    • Stp1p, Stp2p and Abf1 p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae
    • de Boer M, Nielsen PS, Bebelman JP, Heerikhuizen H, Andersen HA, Planta RJ (2000) Stp1p, Stp2p and Abf1 p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae. Nucleic Acids Res 28: 974-981
    • (2000) Nucleic Acids Res , vol.28 , pp. 974-981
    • de Boer, M.1    Nielsen, P.S.2    Bebelman, J.P.3    Heerikhuizen, H.4    Andersen, H.A.5    Planta, R.J.6
  • 10
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane
    • Dreger M, Bengtsson L, Schoneberg T, Otto H, Hucho F (2001) Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci USA 98: 11943-11948
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schoneberg, T.3    Otto, H.4    Hucho, F.5
  • 11
    • 0032793068 scopus 로고    scopus 로고
    • Regulation of peroxisome proliferator-activated receptor γ expression by adipocyte differentiation and determination factor 1/sterol regulatory element binding protein 1: Implications for adipocyte differentiation and metabolism
    • Fajas L, Schoonjans K, Gelman L, Kim JB, Najib J, Martin G, Fruchart JC, Briggs M, Spiegelman BM, Auwerx J (1999) Regulation of peroxisome proliferator-activated receptor γ expression by adipocyte differentiation and determination factor 1/sterol regulatory element binding protein 1: Implications for adipocyte differentiation and metabolism. Mol Cell Biol 19: 5495-5503
    • (1999) Mol Cell Biol , vol.19 , pp. 5495-5503
    • Fajas, L.1    Schoonjans, K.2    Gelman, L.3    Kim, J.B.4    Najib, J.5    Martin, G.6    Fruchart, J.C.7    Briggs, M.8    Spiegelman, B.M.9    Auwerx, J.10
  • 12
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R, Gerace I. (1993) Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73: 1267-1279
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, I.2
  • 13
    • 0034918712 scopus 로고    scopus 로고
    • Suppressors of ssy1 and ptr3 null mutations define novel amino acid sensor-independent genes in Saccharomyces cerevisiae
    • Forsberg H, Hammar M, Andreasson C, Moliner A, Ljungdahl PO (2001) Suppressors of ssy1 and ptr3 null mutations define novel amino acid sensor-independent genes in Saccharomyces cerevisiae. Genetics 158: 973-988
    • (2001) Genetics , vol.158 , pp. 973-988
    • Forsberg, H.1    Hammar, M.2    Andreasson, C.3    Moliner, A.4    Ljungdahl, P.O.5
  • 14
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • s
    • Franke WW, Scheer U, Krohne G, Jarasch ED (1981) The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol 91 39S-50s
    • (1981) J Cell Biol , vol.91
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.D.4
  • 16
    • 1542284570 scopus 로고    scopus 로고
    • Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy
    • Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y (2004) Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy, Eur J Biochem 271: 1035-1045
    • (2004) Eur J Biochem , vol.271 , pp. 1035-1045
    • Haraguchi, T.1    Holaska, J.M.2    Yamane, M.3    Koujin, T.4    Hashiguchi, N.5    Mori, C.6    Wilson, K.L.7    Hiraoka, Y.8
  • 17
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • Holaska JM, Lee KK, Kowalski AK, Wilson KL (2003) Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 278 6969-6975
    • (2003) J Biol Chem , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 18
    • 0030681031 scopus 로고    scopus 로고
    • Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression
    • Imai S, Nishibayashi S, Takao K, Tomifuji M, Fujino T, Hasegawa M, Takano T (1997) Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression. Mol Boil Cell 8: 2407-2419
    • (1997) Mol Boil Cell , vol.8 , pp. 2407-2419
    • Imai, S.1    Nishibayashi, S.2    Takao, K.3    Tomifuji, M.4    Fujino, T.5    Hasegawa, M.6    Takano, T.7
  • 19
    • 33750429896 scopus 로고    scopus 로고
    • Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor β signaling
    • Ishimura A, Ng JK, Taira M, Young SG, Osada S (2006) Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor β signaling. Development 133: 3919-3928
    • (2006) Development , vol.133 , pp. 3919-3928
    • Ishimura, A.1    Ng, J.K.2    Taira, M.3    Young, S.G.4    Osada, S.5
  • 22
    • 0033008195 scopus 로고    scopus 로고
    • Btf, a novel death-promoting tanscriptional repressor that interacts with Bcl-2-related proteins
    • Kasof GM, Goyal L, White E (1999) Btf, a novel death-promoting tanscriptional repressor that interacts with Bcl-2-related proteins. Mol Cell Biol 19: 4390-4404
    • (1999) Mol Cell Biol , vol.19 , pp. 4390-4404
    • Kasof, G.M.1    Goyal, L.2    White, E.3
  • 23
    • 0037049554 scopus 로고    scopus 로고
    • Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription
    • Kumaran RI, Muralikrishna B, Pamaik VK (2002) Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription. J Cell Biol 159: 783-793
    • (2002) J Cell Biol , vol.159 , pp. 783-793
    • Kumaran, R.I.1    Muralikrishna, B.2    Pamaik, V.K.3
  • 25
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-β signaling
    • Lin F, Morrison JM, Wu W, Worman HJ (2005) MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-β signaling. Hum Mol Genet 14: 437-45
    • (2005) Hum Mol Genet , vol.14 , pp. 437-445
    • Lin, F.1    Morrison, J.M.2    Wu, W.3    Worman, H.J.4
  • 26
    • 17144380019 scopus 로고    scopus 로고
    • Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor
    • Mansharamani M, Wilson KL (2005) Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. J Biol Chem 280: 13863-13870
    • (2005) J Biol Chem , vol.280 , pp. 13863-13870
    • Mansharamani, M.1    Wilson, K.L.2
  • 27
    • 1842854443 scopus 로고    scopus 로고
    • Lamin A/C binding protein LAP2α is required for nuclear anchorage of retinoblastoma protein
    • Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (2002) Lamin A/C binding protein LAP2α is required for nuclear anchorage of retinoblastoma protein. Mol Biol Cell 13: 4401-4413
    • (2002) Mol Biol Cell , vol.13 , pp. 4401-4413
    • Markiewicz, E.1    Dechat, T.2    Foisner, R.3    Quinlan, R.A.4    Hutchison, C.J.5
  • 28
    • 33746500691 scopus 로고    scopus 로고
    • The inner nuclear membrane protein emerin regulates β-catenin activity by restricting its accumulation in the nucleus
    • Markiewicz E et al (2006) The inner nuclear membrane protein emerin regulates β-catenin activity by restricting its accumulation in the nucleus. EMBO J 25: 3275-3285
    • (2006) EMBO J , vol.25 , pp. 3275-3285
    • Markiewicz, E.1
  • 31
    • 0034777991 scopus 로고    scopus 로고
    • Nuclear membrane protein LAP2β mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)
    • Nili E et al (2001) Nuclear membrane protein LAP2β mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less). J Cell Sci 114: 3297-3307
    • (2001) J Cell Sci , vol.114 , pp. 3297-3307
    • Nili, E.1
  • 32
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada S, Ohmori SY, Taira M (2003) XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development 130: 1783-1794
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.1    Ohmori, S.Y.2    Taira, M.3
  • 33
    • 18144411595 scopus 로고    scopus 로고
    • The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-β superfamily of cytokines
    • Pan D, Estevez-Salmeron LD, Stroschein SL, Zhu X, He J, Zhou S, Luo K (2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-β superfamily of cytokines. J Biol Chem 280: 15992-16001
    • (2005) J Biol Chem , vol.280 , pp. 15992-16001
    • Pan, D.1    Estevez-Salmeron, L.D.2    Stroschein, S.L.3    Zhu, X.4    He, J.5    Zhou, S.6    Luo, K.7
  • 35
    • 25144491496 scopus 로고    scopus 로고
    • The nuclear membrane proteome: Extending the envelope
    • Schirmer EC, Gerace L (2005) The nuclear membrane proteome: Extending the envelope. Trends Biochem Sci 30: 551-558
    • (2005) Trends Biochem Sci , vol.30 , pp. 551-558
    • Schirmer, E.C.1    Gerace, L.2
  • 36
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301: 1380-1382
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 37
    • 0037128211 scopus 로고    scopus 로고
    • Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription
    • Spann TP, Goldman AE, Wang C, Huang S, Goldman RD (2002) Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription. J. Cell Biol 156: 603-608
    • (2002) J. Cell Biol , vol.156 , pp. 603-608
    • Spann, T.P.1    Goldman, A.E.2    Wang, C.3    Huang, S.4    Goldman, R.D.5
  • 38
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • Stuurman N, Heins S, Aebi U (1998) Nuclear lamins: Their structure, assembly, and interactions. J Struct Biol 122: 42-66
    • (1998) J Struct Biol , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 39
    • 33746942748 scopus 로고    scopus 로고
    • Inner nuclear membrane and regulation of Smad-mediated signaling
    • Worman HJ (2006) Inner nuclear membrane and regulation of Smad-mediated signaling. Biochim Biophys Acta 1761: 626-631
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 626-631
    • Worman, H.J.1
  • 40
    • 33847007692 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert to maintain the latent properties of transcription factors Stp1 and Stp2
    • Zargari A, Boban M, Heessen S, Andreasson C, Thyberg J, Ljungdahl PO (2007) Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert to maintain the latent properties of transcription factors Stp1 and Stp2. J Biol Chem 282: 594-605
    • (2007) J Biol Chem , vol.282 , pp. 594-605
    • Zargari, A.1    Boban, M.2    Heessen, S.3    Andreasson, C.4    Thyberg, J.5    Ljungdahl, P.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.