The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Mcl‐1; the molecular regulation of protein function
Abstract
Apoptosis, an essential and basic biological phenomenon, is regulated in a complex manner by a multitude of factors. Myeloid cell leukemia 1 (Mcl‐1), an anti‐apoptotic member of the B‐cell lymphoma 2 (Bcl‐2) family of apoptosis‐regulating proteins, exemplifies a number of the mechanisms by which a protein's contribution to cell fate may be modified. The N‐terminus of Mcl‐1 is unique amongst the Bcl‐2 family, in that it is rich in experimentally confirmed and putative regulatory residues and motifs. These include sites for ubiquitination, cleavage and phosphorylation, which influence the protein's stability, localisation, dimerization and function. Here we review what is known about the regulation of Mcl‐1 expression and function, with particular focus on post‐translational modifications and how phosphorylation interconnects the complex molecular control of Mcl‐1 with cellular state.
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Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628
Mcl-1 deficiency results in peri-implantation embryonic lethality
Rinkenberger, J. L., Horning, S., Klocke, B., Roth, K., & Korsmeyer, S. J. (2000) · Genes & Development · doi:10.1101/gad.14.1.23 · Cited by 397
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Phosphorylation and Inactivation of Myeloid Cell Leukemia 1 by JNK in Response to Oxidative Stress
Inoshita, S., Takeda, K., Hatai, T., Terada, Y., Sano, M., Hata, J., Umezawa, A., & Ichijo, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207951200 · Cited by 233
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Mcl-1 Integrates the Opposing Actions of Signaling Pathways That Mediate Survival and Apoptosis
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Cited by
Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy
Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219
Tron, A. E., Belmonte, M. A., Adam, A., Aquila, B. M., Boise, L. H., Chiarparin, E., Cidado, J., Embrey, K. J., Gangl, E., Gibbons, F. D., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07551-w · Cited by 490
Apoptosis in Alzheimer’s disease: Insight into the signaling pathways and therapeutic avenues
Kumari, S., Dhapola, R., & Reddy, D. H. (2023) · Apoptosis · doi:10.1007/s10495-023-01848-y · Cited by 324
Franco, J., Balaji, U., Freinkman, E., Witkiewicz, A. K., & Knudsen, E. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.094 · Cited by 199
Basu, A. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107943 · Cited by 171
Metadata
- Authors
- Thomas, L. W., Lam, C., & Edwards, S. W.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2010-06-09
- Volume
- 584
- Issue
- 14
- Pages
- 2981-2989
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1982254984
- Cited by
- 538
- References
- 9
- FWCI
- 11.46
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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