메뉴 건너뛰기




Volumn 22, Issue 17, 2013, Pages 3498-3507

Corrigendum to Dyskeratosis congenita mutations in dyskerin sumoylation consensus sites lead to impaired telomerase RNA accumulation and telomere defects [Human Molecular Genetics 22, 17, (2013) 3498-3507] DOI: 10.1093/hmg/ddt204;Dyskeratosis congenita mutations in dyskerin SUMOylation consensus sites lead to impaired telomerase RNA accumulation and telomere defects

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; DYSKERIN; MESSENGER RNA; RNA; SHORT HAIRPIN RNA; SULFUR 35; TELOMERASE;

EID: 84881574830     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt506     Document Type: Erratum
Times cited : (21)

References (52)
  • 1
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • Palm, W. and de Lange, T. (2008) How shelterin protects mammalian telomeres. Annu. Rev. Genet., 42, 301-334.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 301-334
    • Palm, W.1    de Lange, T.2
  • 2
    • 0029128798 scopus 로고
    • Telomerase and DNA end replication: not a lagging strand problem
    • Lingner, J., Cooper, J.P., Cech, T.R. (1995) Telomerase and DNA end replication: not a lagging strand problem. Science, 269, 1533-1534.
    • (1995) Science , vol.269 , pp. 1533-1534
    • Lingner, J.1    Cooper, J.P.2    Cech, T.R.3
  • 3
    • 33745849998 scopus 로고    scopus 로고
    • The structure and function of telomerase reverse transcriptase
    • Autexier, C., Lue, N. (2006) The structure and function of telomerase reverse transcriptase. Ann. Rev. Biochem., 75, 493-517.
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 493-517
    • Autexier, C.1    Lue, N.2
  • 4
    • 0035253526 scopus 로고    scopus 로고
    • Stable expression in yeast of the mature form of human telomerase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p
    • Dez, C., Henras, A., Faucon, B., Lafontaine, D.L.J., Caizergues-Ferrer, M., Henry, Y. (2001) Stable expression in yeast of the mature form of human telomerase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p. Nucl. Acids Res., 29, 598-603.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 598-603
    • Dez, C.1    Henras, A.2    Faucon, B.3    Lafontaine, D.L.J.4    Caizergues-Ferrer, M.5    Henry, Y.6
  • 5
    • 0033518188 scopus 로고    scopus 로고
    • A telomerase component is defective in the human disease dyskeratosis congenita
    • Mitchell, J.R., Wood, E., Collins, K. (1999) A telomerase component is defective in the human disease dyskeratosis congenita. Nature, 402, 551-555.
    • (1999) Nature , vol.402 , pp. 551-555
    • Mitchell, J.R.1    Wood, E.2    Collins, K.3
  • 6
    • 45849131292 scopus 로고    scopus 로고
    • Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita
    • Vulliamy, T., Beswick, R., Kirwan, M., Marrone, A., Digweed, M., Walne, A., Dokal, I. (2008) Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita. Proc. Natl Acad. Sci. USA, 105, 8073-8078.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8073-8078
    • Vulliamy, T.1    Beswick, R.2    Kirwan, M.3    Marrone, A.4    Digweed, M.5    Walne, A.6    Dokal, I.7
  • 7
    • 34447307404 scopus 로고    scopus 로고
    • Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations inthe telomerase-associated protein NOP10
    • Walne, A.J., Vulliamy, T., Marrone, A., Beswick, R., Kirwan, M., Masunari, Y., Al-Qurashi, F.H., Aljurf, M., Dokal, I. (2007) Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations inthe telomerase-associated protein NOP10. Hum. Mol. Genet., 16, 1619-1629.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1619-1629
    • Walne, A.J.1    Vulliamy, T.2    Marrone, A.3    Beswick, R.4    Kirwan, M.5    Masunari, Y.6    Al-Qurashi, F.H.7    Aljurf, M.8    Dokal, I.9
  • 8
    • 40749135820 scopus 로고    scopus 로고
    • Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly
    • Venteicher, A.S., Meng, Z., Mason, P.J., Veenstra, T.D., Artandi, S.E. (2008) Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly. Cell, 132, 945-957.
    • (2008) Cell , vol.132 , pp. 945-957
    • Venteicher, A.S.1    Meng, Z.2    Mason, P.J.3    Veenstra, T.D.4    Artandi, S.E.5
  • 11
    • 84855486059 scopus 로고    scopus 로고
    • Dyskeratosis congenita as a disorder of telomere maintenance
    • Nelson, N.D., Bertuch, A.A. (2012) Dyskeratosis congenita as a disorder of telomere maintenance. Mutat. Res., 730, 43-51.
    • (2012) Mutat. Res. , vol.730 , pp. 43-51
    • Nelson, N.D.1    Bertuch, A.A.2
  • 12
    • 34547410832 scopus 로고    scopus 로고
    • Dyskeratosis congenita: advances in the understanding of the telomerase defect and the role of stem cell transplantation
    • de la Fuente, J., Dokal, I. (2007) Dyskeratosis congenita: advances in the understanding of the telomerase defect and the role of stem cell transplantation. Pediatr. Transplant., 11, 584-594.
    • (2007) Pediatr. Transplant. , vol.11 , pp. 584-594
    • de la Fuente, J.1    Dokal, I.2
  • 13
    • 0031799895 scopus 로고    scopus 로고
    • X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions
    • Heiss, N.S., Knight, S.W., Vulliamy, T., Klauck, S.M.,Wiemann, S., Mason, P.J., Poustka, A., Dokal, I. (1998) X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Nature, 19, 32-38.
    • (1998) Nature , vol.19 , pp. 32-38
    • Heiss, N.S.1    Knight, S.W.2    Vulliamy, T.3    Klauck, S.M.4    Wiemann, S.5    Mason, P.J.6    Poustka, A.7    Dokal, I.8
  • 14
    • 33751072682 scopus 로고    scopus 로고
    • Telomerase RNA level limits telomere maintenance in X-linked dyskeratosis congenita
    • Wong, J.M., Collins, K. (2006) Telomerase RNA level limits telomere maintenance in X-linked dyskeratosis congenita. Genes Dev., 20, 2848-2858.
    • (2006) Genes Dev. , vol.20 , pp. 2848-2858
    • Wong, J.M.1    Collins, K.2
  • 15
    • 19444383162 scopus 로고    scopus 로고
    • Dyskeratosis congenita: telomerase, telomeres and anticipation
    • Marrone, A., Walne, A., Dokal, I. (2005) Dyskeratosis congenita: telomerase, telomeres and anticipation. Curr. Opin. Gen. Dev., 15, 249-257. 16. Li, L., Ye, K. (2006) Crystal structure of an H/ACA box ribonucleoprotein particle. Nature, 443, 302-307.
    • (2005) Curr. Opin. Gen. Dev. , vol.15 , pp. 249-257
    • Marrone, A.1    Walne, A.2    Dokal, I.3
  • 16
    • 33748947672 scopus 로고    scopus 로고
    • Crystal structure of an H/ACA box ribonucleoprotein particle
    • Li, L., Ye, K. (2006) Crystal structure of an H/ACA box ribonucleoprotein particle. Nature, 443, 302-307.
    • (2006) Nature , vol.443 , pp. 302-307
    • Li, L.1    Ye, K.2
  • 17
    • 77950525937 scopus 로고    scopus 로고
    • Effects of dyskeratosis congenita mutations in dyskerin, NHP2 and NOP10 on assembly of H/ACA pre-RNPs
    • Trahan, C., Martel, C., Dragon, F. (2010) Effects of dyskeratosis congenita mutations in dyskerin, NHP2 and NOP10 on assembly of H/ACA pre-RNPs. Hum. Mol. Genet., 19, 825-836.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 825-836
    • Trahan, C.1    Martel, C.2    Dragon, F.3
  • 18
    • 84856364779 scopus 로고    scopus 로고
    • The accumulation and not the specific activity of telomerase ribonucleoprotein determines telomere maintenance deficiency in X-linked dyskeratosis congenita
    • Zeng, X.L., Thumati, N.R., Fleisig, H.B., Hukezalie, K.R., Savage, S.A., Giri, N., Alter, B.P., Wong, J.M. (2011) The accumulation and not the specific activity of telomerase ribonucleoprotein determines telomere maintenance deficiency in X-linked dyskeratosis congenita. Hum. Mol. Genet., 21, 721-729.
    • (2011) Hum. Mol. Genet. , vol.21 , pp. 721-729
    • Zeng, X.L.1    Thumati, N.R.2    Fleisig, H.B.3    Hukezalie, K.R.4    Savage, S.A.5    Giri, N.6    Alter, B.P.7    Wong, J.M.8
  • 19
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J.R., Lima, C.D. (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol., 11, 861-871.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 20
    • 55249096736 scopus 로고    scopus 로고
    • The fast-growing business of SUMO chains
    • Ulrich, H.D. (2008) The fast-growing business of SUMO chains. Mol. Cell, 32, 301-305.
    • (2008) Mol. Cell , vol.32 , pp. 301-305
    • Ulrich, H.D.1
  • 21
    • 55249095331 scopus 로고    scopus 로고
    • Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution
    • Matic, I., Macek, B., Hilger, M., Walther, T.C., Mann, M. (2008) Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution. J. Proteome Res., 7, 4050-4057.
    • (2008) J. Proteome Res. , vol.7 , pp. 4050-4057
    • Matic, I.1    Macek, B.2    Hilger, M.3    Walther, T.C.4    Mann, M.5
  • 22
    • 77955990555 scopus 로고    scopus 로고
    • A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58
    • Westman, B.J., Verheggen, C., Hutten, S., Lam, Y.W., Bertrand, E., Lamond, A.I. (2010) A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58. Mol. Cell, 39, 618-631.
    • (2010) Mol. Cell , vol.39 , pp. 618-631
    • Westman, B.J.1    Verheggen, C.2    Hutten, S.3    Lam, Y.W.4    Bertrand, E.5    Lamond, A.I.6
  • 24
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of proteinSUMOylation: Development of a site-specific predictor of SUMOsp 2
    • Ren, J., Gao, X., Jin, C., Zhu, M., Wang, X., Shaw, A., Wen, L., Yao, X., Xue, Y. (2009) Systematic study of proteinSUMOylation: Development of a site-specific predictor of SUMOsp 2.0. Proteomics, 9, 3409-3412.
    • (2009) 0. Proteomics , vol.9 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3    Zhu, M.4    Wang, X.5    Shaw, A.6    Wen, L.7    Yao, X.8    Xue, Y.9
  • 25
    • 0032754538 scopus 로고    scopus 로고
    • Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita
    • Heiss, N.S., Girod, A., Salowsky, R., Wiemann, S., Pepperkok, R., Poustka, A. (1999) Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita. Hum. Mol. Genet., 8, 2515-2524.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2515-2524
    • Heiss, N.S.1    Girod, A.2    Salowsky, R.3    Wiemann, S.4    Pepperkok, R.5    Poustka, A.6
  • 26
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic, I., Schimmel, J., Hendriks, I.A., van Santen, M.A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., Vertegaal, A.C. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell, 39, 641-652.
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    van Santen, M.A.4    van de Rijke, F.5    van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.9
  • 27
    • 0036435057 scopus 로고    scopus 로고
    • A novel DKC1 mutation, severe combined immunodeficiency (T+B-NK- SCID) and bone marrow transplantation in an infant with Hoyeraal-Hreidarsson syndrome
    • Cossu, F., Vulliamy, T.J., Marrone, A., Badiali, M., Cao, A., Dokal, I. (2002) A novel DKC1 mutation, severe combined immunodeficiency (T+B-NK- SCID) and bone marrow transplantation in an infant with Hoyeraal-Hreidarsson syndrome. Br. J. Haematol., 119, 765-768.
    • (2002) Br. J. Haematol. , vol.119 , pp. 765-768
    • Cossu, F.1    Vulliamy, T.J.2    Marrone, A.3    Badiali, M.4    Cao, A.5    Dokal, I.6
  • 29
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro, J.M., Thomson, J., Hay, R.T. (1997) Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett., 417, 297-300.
    • (1997) FEBS Lett. , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 31
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M.S., Dargemont, C., Hay, R.T. (2001)SUMO-1conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem., 276, 12654-12659.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 32
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson, D.A.,Wang,M.and Matunis, M.J. (2001)The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem., 276, 21664-21669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 33
    • 47549109045 scopus 로고    scopus 로고
    • Sumoylation regulates laminAfunction and is lost in lamin A mutants associated with familial cardiomyopathies
    • Zhang, Y.Q., Sarge, K.D. (2008) Sumoylation regulates laminAfunction and is lost in lamin A mutants associated with familial cardiomyopathies. J. Cell Biol., 182, 35-39.
    • (2008) J. Cell Biol. , vol.182 , pp. 35-39
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 35
    • 80052765356 scopus 로고    scopus 로고
    • SUMOylation and de-SUMOylation in response to DNA damage
    • Dou, H., Huang, C., Van Nguyen, T., Lu, L.S., Yeh, E.T. (2011) SUMOylation and de-SUMOylation in response to DNA damage. FEBS Lett., 585, 2891-2896.
    • (2011) FEBS Lett. , vol.585 , pp. 2891-2896
    • Dou, H.1    Huang, C.2    Van Nguyen, T.3    Lu, L.S.4    Yeh, E.T.5
  • 36
    • 1842844308 scopus 로고    scopus 로고
    • Repression of Smad4 transcriptional activity by SUMO modification
    • Long, J., Wang, G., He, D., Liu, F. (2004) Repression of Smad4 transcriptional activity by SUMO modification. Biochem. J., 379, 23-29.
    • (2004) Biochem. J. , vol.379 , pp. 23-29
    • Long, J.1    Wang, G.2    He, D.3    Liu, F.4
  • 37
    • 33646838989 scopus 로고    scopus 로고
    • Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription
    • Spengler, M.L., Brattain, M.G. (2006) Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription. J. Biol. Chem., 281, 5567-5574.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5567-5574
    • Spengler, M.L.1    Brattain, M.G.2
  • 38
    • 72749119233 scopus 로고    scopus 로고
    • Single-molecule analysis of the human telomerase RNA dyskerin interaction and the effect of dyskeratosis congenita mutations.
    • Ashbridge, B., Orte, A., Yeoman, J.A., Kirwan, M., Vulliamy, T., Dokal, I., Klenerman,D., Balasubramanian, S. (2009) Single-molecule analysis of the human telomerase RNA.dyskerin interaction and the effect of dyskeratosis congenita mutations. Biochemistry (Mosc), 48, 10858-10865.
    • (2009) Biochemistry (Mosc) , vol.48 , pp. 10858-10865
    • Ashbridge, B.1    Orte, A.2    Yeoman, J.A.3    Kirwan, M.4    Vulliamy, T.5    Dokal, I.6    Klenerman, D.7    Balasubramanian, S.8
  • 39
    • 79955526833 scopus 로고    scopus 로고
    • Decreased dyskerin levels as a mechanism of telomere shortening in X-linked dyskeratosis congenita
    • Parry, E.M., Alder, J.K., Lee, S.S., Phillips, J.A. III, Loyd, J.E., Duggal, P., Armanios, M. (2011) Decreased dyskerin levels as a mechanism of telomere shortening in X-linked dyskeratosis congenita. J. Med. Genet., 48, 327-333.
    • (2011) J. Med. Genet. , vol.48 , pp. 327-333
    • Parry, E.M.1    Alder, J.K.2    Lee, S.S.3    Phillips, J.A.4    Loyd, J.E.5    Duggal, P.6    Armanios, M.7
  • 40
    • 34547113757 scopus 로고    scopus 로고
    • Sumoylation of Oct4 enhances its stability,DNAbinding, and transactivation
    • Wei, F., Scholer, H.R., Atchison, M.L. (2007) Sumoylation of Oct4 enhances its stability,DNAbinding, and transactivation. J. Biol. Chem., 282, 21551-21560.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21551-21560
    • Wei, F.1    Scholer, H.R.2    Atchison, M.L.3
  • 43
    • 84866611481 scopus 로고    scopus 로고
    • Biogenesis of telomerase ribonucleoproteins
    • Egan, E.D., Collins, K. (2012) Biogenesis of telomerase ribonucleoproteins. RNA., 18, 1747-1759.
    • (2012) RNA. , vol.18 , pp. 1747-1759
    • Egan, E.D.1    Collins, K.2
  • 44
    • 66449111635 scopus 로고    scopus 로고
    • SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs
    • Grozdanov, P.N., Roy, S., Kittur, N., Meier, U.T. (2009) SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs. RNA, 15, 1188-1197.
    • (2009) RNA , vol.15 , pp. 1188-1197
    • Grozdanov, P.N.1    Roy, S.2    Kittur, N.3    Meier, U.T.4
  • 45
    • 84866604898 scopus 로고    scopus 로고
    • Mechanism of theAAA+ ATPases pontin and reptin in the biogenesis of H/ ACA RNPs
    • Machado-Pinilla, R., Liger, D., Leulliot, N., Meier, U.T. (2012) Mechanism of theAAA+ ATPases pontin and reptin in the biogenesis of H/ ACA RNPs. RNA, 18, 1833-1845.
    • (2012) RNA , vol.18 , pp. 1833-1845
    • Machado-Pinilla, R.1    Liger, D.2    Leulliot, N.3    Meier, U.T.4
  • 47
    • 70449403276 scopus 로고    scopus 로고
    • Pathogenic NAP57 mutations decrease ribonucleoprotein assembly in dyskeratosis congenita
    • Grozdanov, P.N., Fernandez-Fuentes, N., Fiser, A., Meier, U.T. (2009) Pathogenic NAP57 mutations decrease ribonucleoprotein assembly in dyskeratosis congenita. Hum. Mol. Genet., 18, 4546-4551.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4546-4551
    • Grozdanov, P.N.1    Fernandez-Fuentes, N.2    Fiser, A.3    Meier, U.T.4
  • 48
    • 5044251217 scopus 로고    scopus 로고
    • Telomerase RNA deficiency in peripheral blood mononuclear cells in X-linked dyskeratosis congenita
    • Wong, J.M., Kyasa, M.J., Hutchins, L., Collins, K. (2004) Telomerase RNA deficiency in peripheral blood mononuclear cells in X-linked dyskeratosis congenita. Hum. Genet., 115, 448-455.
    • (2004) Hum. Genet. , vol.115 , pp. 448-455
    • Wong, J.M.1    Kyasa, M.J.2    Hutchins, L.3    Collins, K.4
  • 52
    • 39349106809 scopus 로고    scopus 로고
    • Quantitative fluorescence in situ hybridization (Q-FISH)
    • Poon, S.S., Lansdorp, P.M. (2001) Quantitative fluorescence in situ hybridization (Q-FISH). Curr. Protoc. Cell Biol., 18, 1-21
    • (2001) Curr. Protoc. Cell Biol. , vol.18 , pp. 1-21
    • Poon, S.S.1    Lansdorp, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.