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Volumn 54, Issue 3-4, 2009, Pages 245-252

NAC1, a POZ/BTB protein that functions as a corepressor

Author keywords

Coimmunoprecipitations; GST pulldowns; In vitro translation; Nucleus accumbens; Transcriptional repressor

Indexed keywords

ACTIN BINDING PROTEIN; BCOR PROTEIN; HYBRID PROTEIN; MAYVEN PROTEIN; NAC1 PROTEIN; NRP PROTEIN; PROTEIN BCL 6; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR GAL4; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN 5;

EID: 60949105690     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2008.12.008     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 14844282882 scopus 로고    scopus 로고
    • The superfamily of proteins containing kelch and/or BTB domains: from cytoskeleton dynamics to transcriptional regulation
    • Avraham S.A.H., Jiang S., Bu X., Liang X.-Q., Seng S., and Kim T. The superfamily of proteins containing kelch and/or BTB domains: from cytoskeleton dynamics to transcriptional regulation. Recent Res. Dev. Biol. Chem. 1 (2002) 231254
    • (2002) Recent Res. Dev. Biol. Chem. , vol.1 , pp. 231254
    • Avraham, S.A.H.1    Jiang, S.2    Bu, X.3    Liang, X.-Q.4    Seng, S.5    Kim, T.6
  • 3
    • 0029099016 scopus 로고
    • The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins
    • Albagli O., Dhordain P., Deweindt C., Lecocq G., and Leprince D. The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins. Cell Growth Differ. 6 (1995) 1193-1198
    • (1995) Cell Growth Differ. , vol.6 , pp. 1193-1198
    • Albagli, O.1    Dhordain, P.2    Deweindt, C.3    Lecocq, G.4    Leprince, D.5
  • 5
    • 0030870436 scopus 로고    scopus 로고
    • NAC-1, a rat brain mRNA, is increased in the nucleus accumbens three weeks after chronic cocaine self-administration
    • Cha X.Y., Pierce R.C., Kalivas P.W., and Mackler S.A. NAC-1, a rat brain mRNA, is increased in the nucleus accumbens three weeks after chronic cocaine self-administration. J. Neurosci. 17 (1997) 6864-6871
    • (1997) J. Neurosci. , vol.17 , pp. 6864-6871
    • Cha, X.Y.1    Pierce, R.C.2    Kalivas, P.W.3    Mackler, S.A.4
  • 6
    • 0037163043 scopus 로고    scopus 로고
    • Actinfilin, a brain-specific actin-binding protein in postsynaptic density
    • Chen Y., Derin R., Petralia R.S., and Li M. Actinfilin, a brain-specific actin-binding protein in postsynaptic density. J. Biol. Chem. 277 (2002) 30495-30501
    • (2002) J. Biol. Chem. , vol.277 , pp. 30495-30501
    • Chen, Y.1    Derin, R.2    Petralia, R.S.3    Li, M.4
  • 7
    • 0034999879 scopus 로고    scopus 로고
    • All in the family: the BTB/POZ, KRAB, and SCAN domains
    • Collins T., Stone J.R., and Williams A.J. All in the family: the BTB/POZ, KRAB, and SCAN domains. Mol. Cell Biol. 21 (2001) 3609-3615
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3609-3615
    • Collins, T.1    Stone, J.R.2    Williams, A.J.3
  • 8
    • 0033593036 scopus 로고    scopus 로고
    • Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B
    • Deltour S., Guerardel C., and Leprince D. Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 14831-14836
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14831-14836
    • Deltour, S.1    Guerardel, C.2    Leprince, D.3
  • 9
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R., Wee S., Anderson S., Yates J., and Wolf D.A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12 (2003) 783-790
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 11
    • 0032511890 scopus 로고    scopus 로고
    • The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT
    • Huynh K.D., and Bardwell V.J. The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT. Oncogene 17 (1998) 2473-2484
    • (1998) Oncogene , vol.17 , pp. 2473-2484
    • Huynh, K.D.1    Bardwell, V.J.2
  • 12
    • 0034661112 scopus 로고    scopus 로고
    • BCoR, a novel corepressor involved in BCL-6 repression
    • Huynh K.D., Fischle W., Verdin E., and Bardwell V.J. BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 14 (2000) 1810-1823
    • (2000) Genes Dev. , vol.14 , pp. 1810-1823
    • Huynh, K.D.1    Fischle, W.2    Verdin, E.3    Bardwell, V.J.4
  • 13
    • 14844282064 scopus 로고    scopus 로고
    • Process elongation of oligodendrocytes is promoted by the Kelch-related actin-binding protein Mayven
    • Jiang S., Avraham H.K., Park S.Y., Kim T.A., Bu X., Seng S., and Avraham S. Process elongation of oligodendrocytes is promoted by the Kelch-related actin-binding protein Mayven. J. Neurochem. 92 (2005) 1191-1203
    • (2005) J. Neurochem. , vol.92 , pp. 1191-1203
    • Jiang, S.1    Avraham, H.K.2    Park, S.Y.3    Kim, T.A.4    Bu, X.5    Seng, S.6    Avraham, S.7
  • 14
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang M.I., Kobayashi A., Wakabayashi N., Kim S.G., and Yamamoto M. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2046-2051
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 15
    • 0032482230 scopus 로고    scopus 로고
    • NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation
    • Kim T.A., Lim J., Ota S., Raja S., Rogers R., Rivnay B., Avraham H., and Avraham S. NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation. J. Cell Biol. 141 (1998) 553-566
    • (1998) J. Cell Biol. , vol.141 , pp. 553-566
    • Kim, T.A.1    Lim, J.2    Ota, S.3    Raja, S.4    Rogers, R.5    Rivnay, B.6    Avraham, H.7    Avraham, S.8
  • 16
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T., Igarashi K., and Yamamoto M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell Biol. 24 (2004) 7130-7139
    • (2004) Mol. Cell Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 19
    • 34247328562 scopus 로고    scopus 로고
    • NAC1, a cocaine-regulated POZ/BTB protein interacts with CoREST
    • Korutla L., Degnan R., Wang P., and Mackler S.A. NAC1, a cocaine-regulated POZ/BTB protein interacts with CoREST. J. Neurochem. 101 (2007) 611-618
    • (2007) J. Neurochem. , vol.101 , pp. 611-618
    • Korutla, L.1    Degnan, R.2    Wang, P.3    Mackler, S.A.4
  • 20
    • 23244441140 scopus 로고    scopus 로고
    • The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal-like cultures
    • Korutla L., Wang P.J., and Mackler S.A. The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal-like cultures. J. Neurochem. 94 (2005) 786-793
    • (2005) J. Neurochem. , vol.94 , pp. 786-793
    • Korutla, L.1    Wang, P.J.2    Mackler, S.A.3
  • 21
    • 0037139295 scopus 로고    scopus 로고
    • Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1
    • Korutla L., Wang P.J., Lewis D.M., Neustadter J.H., Stromberg M.F., and Mackler S.A. Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1. Neuroscience 110 (2002) 421-429
    • (2002) Neuroscience , vol.110 , pp. 421-429
    • Korutla, L.1    Wang, P.J.2    Lewis, D.M.3    Neustadter, J.H.4    Stromberg, M.F.5    Mackler, S.A.6
  • 22
    • 0242525238 scopus 로고    scopus 로고
    • BTB proteins as henchmen of Cul3-based ubiquitin ligases
    • Krek W. BTB proteins as henchmen of Cul3-based ubiquitin ligases. Nat. Cell Biol. 5 (2003) 950-951
    • (2003) Nat. Cell Biol. , vol.5 , pp. 950-951
    • Krek, W.1
  • 23
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the Shaker potassium channel
    • Kreusch A., Pfaffinger P.J., Stevens C.F., and Choe S. Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature 392 (1998) 945-948
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 25
    • 21244481727 scopus 로고    scopus 로고
    • The theoretical basis of transcriptional therapy of cancer: can it be put into practice?
    • Melnick A.M., Adelson K., and Licj J.D. The theoretical basis of transcriptional therapy of cancer: can it be put into practice?. J. Clin. Oncol. 23 (2005) 3957-3970
    • (2005) J. Clin. Oncol. , vol.23 , pp. 3957-3970
    • Melnick, A.M.1    Adelson, K.2    Licj, J.D.3
  • 26
    • 0034268781 scopus 로고    scopus 로고
    • The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel
    • Minor D.L., Lin Y.F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., and Berger J.M. The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel. Cell 102 (2000) 657-670
    • (2000) Cell , vol.102 , pp. 657-670
    • Minor, D.L.1    Lin, Y.F.2    Mobley, B.C.3    Avelar, A.4    Jan, Y.N.5    Jan, L.Y.6    Berger, J.M.7
  • 28
    • 0030766528 scopus 로고    scopus 로고
    • Molecular and cellular basis of addiction
    • Nestler E.J., and Aghajanian G.K. Molecular and cellular basis of addiction. Science 278 (1997) 58-63
    • (1997) Science , vol.278 , pp. 58-63
    • Nestler, E.J.1    Aghajanian, G.K.2
  • 30
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • Pintard L., Willems A., and Peter M. Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. EMBO J. 23 (2004) 1681-1687
    • (2004) EMBO J. , vol.23 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 35
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • Willems A.R., Schwab M., and Tyers M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695 (2004) 133-170
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 36
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu L., Wei Y., Reboul J., Vaglio P., Shin T.H., Vidal M., Elledge S.J., and Harper J.W. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425 (2003) 316-321
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.