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Volumn 491, Issue 1, 2012, Pages 13-19

Acetylation of Prrp K150 regulates the subcellular localization

Author keywords

Acetylation; Germ cells; Nucleocytoplasmic transport; RNA binding protein

Indexed keywords

DELETED AZOOSPERMIA ASSOCIATED PROTEIN 1; LYSINE; PROLINE RICH RNA BINDING PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 80055089204     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.09.022     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 2342580076 scopus 로고    scopus 로고
    • The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity
    • Babic I., Jakymiw A., Fujita D.J. The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity. Oncogene 2004, 23:3781-3789.
    • (2004) Oncogene , vol.23 , pp. 3781-3789
    • Babic, I.1    Jakymiw, A.2    Fujita, D.J.3
  • 2
    • 63449140857 scopus 로고    scopus 로고
    • ELP3 localises to mitochondria and actin-rich domains at edges of HeLa cells
    • Barton D., Braet F., Marc J., Overall R., Gardiner J. ELP3 localises to mitochondria and actin-rich domains at edges of HeLa cells. Neurosci. Lett. 2009, 455:60-64.
    • (2009) Neurosci. Lett. , vol.455 , pp. 60-64
    • Barton, D.1    Braet, F.2    Marc, J.3    Overall, R.4    Gardiner, J.5
  • 4
    • 33745594612 scopus 로고    scopus 로고
    • C-Abl acetylation by histone acetyltransferases regulates its nuclear-cytoplasmic localization
    • di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barilà D. c-Abl acetylation by histone acetyltransferases regulates its nuclear-cytoplasmic localization. EMBO Rep. 2006, 7:727-733.
    • (2006) EMBO Rep. , vol.7 , pp. 727-733
    • di Bari, M.G.1    Ciuffini, L.2    Mingardi, M.3    Testi, R.4    Soddu, S.5    Barilà, D.6
  • 5
    • 66849089384 scopus 로고    scopus 로고
    • P300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization
    • Dietschy T., Shevelev I., Pena-Diaz J., Hühn D., Kuenzle S., Mak R., et al. p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization. J. Cell Sci. 2009, 122:1258-1267.
    • (2009) J. Cell Sci. , vol.122 , pp. 1258-1267
    • Dietschy, T.1    Shevelev, I.2    Pena-Diaz, J.3    Hühn, D.4    Kuenzle, S.5    Mak, R.6
  • 6
    • 0032431026 scopus 로고    scopus 로고
    • HNS, a nuclear-cytoplasmic shuttling sequence in HuR
    • Fan X.C., Steitz J.A. HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:15293-15298.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15293-15298
    • Fan, X.C.1    Steitz, J.A.2
  • 7
    • 44349135730 scopus 로고    scopus 로고
    • Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant
    • Goina E., Skoko N., Pagani F. Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant. Mol. Cell. Biol. 2008, 28:3850-3860.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3850-3860
    • Goina, E.1    Skoko, N.2    Pagani, F.3
  • 8
    • 13744252668 scopus 로고    scopus 로고
    • The RNA ligands for mouse proline-rich RNA-binding protein (mouse Prrp) contain two consensus sequences in separate loop structure
    • Hori T., Taguchi Y., Uesugi S., Kurihara Y., The R.N.A. The RNA ligands for mouse proline-rich RNA-binding protein (mouse Prrp) contain two consensus sequences in separate loop structure. Nucleic Acids Res. 2005, 33:190-200.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 190-200
    • Hori, T.1    Taguchi, Y.2    Uesugi, S.3    Kurihara, Y.4    The, R.N.A.5
  • 9
    • 0035850217 scopus 로고    scopus 로고
    • DNA transfection using linear poly(ethylenimine) prepared by controlled acid hydrolysis of poly(2-ethyl-2-oxazoline)
    • Jeong J.H., Song S.H., Lim D.W., Lee H., Park T.G. DNA transfection using linear poly(ethylenimine) prepared by controlled acid hydrolysis of poly(2-ethyl-2-oxazoline). J. Control Release 2001, 73:391-399.
    • (2001) J. Control Release , vol.73 , pp. 391-399
    • Jeong, J.H.1    Song, S.H.2    Lim, D.W.3    Lee, H.4    Park, T.G.5
  • 10
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 2006, 23:607-618.
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6
  • 11
    • 13444301185 scopus 로고    scopus 로고
    • Dynamic changes in intranuclear and subcellular localizations of mouse Prrp/DAZAP1 during spermatogenesis: the necessity of the C-terminal proline-rich region for nuclear import and localization
    • Kurihara Y., Watanabe H., Kawaguchi A., Hori T., Mishiro K., Ono M., et al. Dynamic changes in intranuclear and subcellular localizations of mouse Prrp/DAZAP1 during spermatogenesis: the necessity of the C-terminal proline-rich region for nuclear import and localization. Arch. Histol. Cytol. 2004, 67:325-333.
    • (2004) Arch. Histol. Cytol. , vol.67 , pp. 325-333
    • Kurihara, Y.1    Watanabe, H.2    Kawaguchi, A.3    Hori, T.4    Mishiro, K.5    Ono, M.6
  • 12
    • 33747609562 scopus 로고    scopus 로고
    • PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription
    • Kuwahara S., Ikei A., Taguchi Y., Tabuchi Y., Fujimoto N., Obinata M., et al. PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription. Biol. Reprod. 2006, 75:352-359.
    • (2006) Biol. Reprod. , vol.75 , pp. 352-359
    • Kuwahara, S.1    Ikei, A.2    Taguchi, Y.3    Tabuchi, Y.4    Fujimoto, N.5    Obinata, M.6
  • 13
    • 33749995013 scopus 로고    scopus 로고
    • Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ
    • Morton S., Yang H.T., Moleleki N., Campbell D.G., Cohen P., Rousseau S. Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ. Biochem. J. 2006, 399:265-273.
    • (2006) Biochem. J. , vol.399 , pp. 265-273
    • Morton, S.1    Yang, H.T.2    Moleleki, N.3    Campbell, D.G.4    Cohen, P.5    Rousseau, S.6
  • 14
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai K., Oubridge C., Jessen T.H., Li J., Evans P.R. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 1990, 348:515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 15
    • 33746565898 scopus 로고    scopus 로고
    • A novel nucleocytoplasmic shuttling sequence of DAZAP1, a testis-abundant RNA-binding protein
    • Lin Y.T., Yen P.H. A novel nucleocytoplasmic shuttling sequence of DAZAP1, a testis-abundant RNA-binding protein. RNA 2006, 12:1486-1493.
    • (2006) RNA , vol.12 , pp. 1486-1493
    • Lin, Y.T.1    Yen, P.H.2
  • 16
    • 0026339487 scopus 로고
    • Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins
    • Piñol-Roma S., Dreyfuss G. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science 1991, 253:312-314.
    • (1991) Science , vol.253 , pp. 312-314
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 17
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi H., Dreyfuss G. A nuclear localization domain in the hnRNP A1 protein. J. Cell Biol. 1995, 129:551-560.
    • (1995) J. Cell Biol. , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 18
    • 79959294504 scopus 로고    scopus 로고
    • DAZAP1, an RNA-binding protein required for development and spermatogenesis, can regulate mRNA translation
    • Smith R.W., Anderson R.C., Smith J.W., Brook M., Richardson W.A., Gray N.K. DAZAP1, an RNA-binding protein required for development and spermatogenesis, can regulate mRNA translation. RNA 2011, 17:1282-1295.
    • (2011) RNA , vol.17 , pp. 1282-1295
    • Smith, R.W.1    Anderson, R.C.2    Smith, J.W.3    Brook, M.4    Richardson, W.A.5    Gray, N.K.6
  • 19
    • 0034192841 scopus 로고    scopus 로고
    • Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1
    • Tsui S., Dai T., Roettger S., Schempp W., Salido E.C., Yen P.H. Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1. Genomics 2000, 65:266-273.
    • (2000) Genomics , vol.65 , pp. 266-273
    • Tsui, S.1    Dai, T.2    Roettger, S.3    Schempp, W.4    Salido, E.C.5    Yen, P.H.6
  • 20
    • 0036708422 scopus 로고    scopus 로고
    • Deleted in azoospermia associated protein 1 shuttles between nucleus and cytoplasm during normal germ cell maturation
    • Vera Y., Dai T., Hikim A.P., Lue Y., Salido E.C., Swerdloff R.S., et al. Deleted in azoospermia associated protein 1 shuttles between nucleus and cytoplasm during normal germ cell maturation. J. Androl. 2002, 23:622-628.
    • (2002) J. Androl. , vol.23 , pp. 622-628
    • Vera, Y.1    Dai, T.2    Hikim, A.P.3    Lue, Y.4    Salido, E.C.5    Swerdloff, R.S.6
  • 21
    • 60549095576 scopus 로고    scopus 로고
    • DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins
    • Yang H.T., Peggie M., Cohen P., Rousseau S. DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins. Biochem. Biophys. Res. Commun. 2009, 380:705-709.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 705-709
    • Yang, H.T.1    Peggie, M.2    Cohen, P.3    Rousseau, S.4
  • 22
    • 0025114362 scopus 로고
    • Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells
    • Yung B.Y., Bor A.M., Chan P.K. Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells. Cancer Res. 1990, 50:5987-5991.
    • (1990) Cancer Res. , vol.50 , pp. 5987-5991
    • Yung, B.Y.1    Bor, A.M.2    Chan, P.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.