The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
A role for the MLL fusion partner ENL in transcriptional elongation and chromatin modification
Open accessAbstract
Chimeric proteins joining the histone methyltransferase MLL with various fusion partners trigger distinctive lymphoid and myeloid leukemias. Here, we immunopurified proteins associated with ENL, a protein commonly fused to MLL. Identification of these ENL-associated proteins (EAPs) by mass spectrometry revealed enzymes with a known role in transcriptional elongation (RNA polymerase II C-terminal domain kinase [RNAPolII CTD] positive transcription elongation factor b [pTEFb]), and in chromatin modification (histone-H3 methyltransferase DOT1L) as well as other frequent MLL partners (AF4, AF5q31, and LAF4), and polycomb group members (RING1, CBX8, and BCoR). The composition of EAP was further verified by coimmunoprecipitation, 2-hybrid analysis, pull-down, and colocalization experiments. Purified EAP showed a histone H3 lysine 79–specific methylase activity, displayed a robust RNAPolII CTD kinase function, and counteracted the effect of the pTEFb inhibitor 5,6-dichloro-benzimidazole-riboside. In vivo, an ENL knock-down diminished genome-wide as well as gene-specific H3K79 dimethylation, reduced global run-on elongation, and inhibited transient transcriptional reporter activity. According to structure-function data, DOT1L recruitment was important for transformation by the MLL-ENL fusion derivative. These results suggest a function of ENL in histone modification and transcriptional elongation.
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Keller, A., Nesvizhskii, A. I., Kolker, E., & Aebersold, R. (2002) · Analytical Chemistry · doi:10.1021/ac025747h · Cited by 4,830
Self-citationA Statistical Model for Identifying Proteins by Tandem Mass Spectrometry
Nesvizhskii, A. I., Keller, A., Kolker, E., & Aebersold, R. (2003) · Analytical Chemistry · doi:10.1021/ac0341261 · Cited by 4,809
Self-citationControlling the elongation phase of transcription with P-TEFb
Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144
Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 865
hDOT1L Links Histone Methylation to Leukemogenesis
Okada, Y., Feng, Q., Lin, Y., Jiang, Q., Li, Y., Coffield, V. M., Su, L., Xu, G., & Zhang, Y. (2005) · Cell · doi:10.1016/j.cell.2005.02.020 · Cited by 804
Monoubiquitination of Human Histone H2B: The Factors Involved and Their Roles in HOX Gene Regulation
Zhu, B., Zheng, Y., Pham, A.-D., Mandal, S. S., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.025 · Cited by 532
BCoR, a novel corepressor involved in BCL-6 repression
Huynh, K. D., Fischle, W., Verdin, E., & Bardwell, V. J. (2000) · Genes & Development · doi:10.1101/gad.14.14.1810 · Cited by 477
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Hoxa9 and Meis1 Are Key Targets for MLL-ENL-Mediated Cellular Immortalization
Zeisig, B. B., Milne, T., García-Cuéllar, M.-P., Schreiner, S., Martin, M.-E., Fuchs, U., Borkhardt, A., Chanda, S. K., Walker, J., Soden, R., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.617-628.2004 · Cited by 328
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Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Shilatifard, A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-134100 · Cited by 1,091
The Global Phosphorylation Landscape of SARS-CoV-2 Infection
Bouhaddou, M., Memon, D., Meyer, B., White, K. M., Rezelj, V. V., Correa Marrero, M., Polacco, B. J., Melnyk, J. E., Ulferts, S., Kaake, R. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.034 · Cited by 1,020
MLL-Rearranged Leukemia Is Dependent on Aberrant H3K79 Methylation by DOT1L
Bernt, K. M., Zhu, N., Sinha, A. U., Vempati, S., Faber, J., Krivtsov, A. V., Feng, Z., Punt, N., Daigle, A., Bullinger, L., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.010 · Cited by 870
Potent inhibition of DOT1L as treatment of MLL-fusion leukemia
Daigle, S. R., Olhava, E. J., Therkelsen, C. A., Basavapathruni, A., Jin, L., Boriack-Sjodin, P. A., Allain, C. J., Klaus, C. R., Raimondi, A., Scott, M. P., et al. (2013) · Blood · doi:10.1182/blood-2013-04-497644 · Cited by 722
Metadata
- Authors
- Mueller, D., Bach, C., Zeisig, D., Garcia-Cuellar, M.-P., Monroe, S., Sreekumar, A., Zhou, R., Nesvizhskii, A., Chinnaiyan, A., Hess, J. L., & Slany, R. K.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2007-12-15
- Volume
- 110
- Issue
- 13
- Pages
- 4445-4454
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W1979316039
- Cited by
- 397
- References
- 31
- FWCI
- 8.38
- Type
- journal article
- Language
- en
- Open access
- green
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