Degradation of LMO2 in T cell leukaemia results in collateral breakdown of transcription complex partners and causes LMO2-dependent apoptosis Article Swipe
Naphannop Sereesongsaeng
,
Carole J. R. Bataille
,
Angela J. Russell
,
Nicolas Béry
,
Fernando J. Sialana
,
Jyoti S. Choudhary
,
Ami Miller
,
Terence H. Rabbitts
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.7554/elife.106699
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.7554/elife.106699
LMO2 is an intrinsically disordered transcription factor activated in T cell leukaemia that is difficult to target. It forms part of a multiprotein complex that has bipartite DNA binding through heterodimeric bHLH and GATA proteins. To determine if degradation of LMO2 in the context of T-ALL has therapeutic potential, a chimaeric intracellular antibody has been developed fusing an anti-LMO2 single domain variable region with one of three E3 ligases to create biodegraders. The intracellular binary interaction of these biodegraders with LMO2 leads to its proteosomal degradation but, in addition, concomitant loss of bHLH proteins that associate with LMO2 in the DNA-binding complex. Chemical compound surrogates of the intracellular antibody paratope (called Abd compounds) have been modified to create proteolysis targeting chimaeras (PROTACs) for orthogonal assays of effects of LMO2 degradation. These form a ternary complex with LMO2 and E3 ligase in leukaemia cells that induces degradation of LMO2, and is also accompanied by loss of associated bHLH proteins. This is accompanied by T-ALL growth inhibition, alterations in proteins involved in cell cycling and instigation of apoptosis. These effects do not occur in the absence of LMO2. Our work demonstrates that degradation of LMO2 affects T-ALL and the lead compounds can eventually be developed into drugs for patient treatment. Our work describes methods for drug discovery starting with antibody fragments.
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.7554/elife.106699
- OA Status
- gold
- References
- 53
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4413008768
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https://doi.org/10.7554/elife.106699Digital Object Identifier
- Title
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Degradation of LMO2 in T cell leukaemia results in collateral breakdown of transcription complex partners and causes LMO2-dependent apoptosisWork title
- Type
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preprintOpenAlex work type
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enPrimary language
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2025Year of publication
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2025-08-06Full publication date if available
- Authors
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Naphannop Sereesongsaeng, Carole J. R. Bataille, Angela J. Russell, Nicolas Béry, Fernando J. Sialana, Jyoti S. Choudhary, Ami Miller, Terence H. RabbittsList of authors in order
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https://doi.org/10.7554/elife.106699Publisher landing page
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://doi.org/10.7554/elife.106699Direct OA link when available
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Ubiquitin ligase, Cell biology, Transcription factor, Ternary complex, Intracellular, Biology, Ubiquitin, Chemistry, Molecular biology, Genetics, Biochemistry, Enzyme, GeneTop concepts (fields/topics) attached by OpenAlex
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0Total citation count in OpenAlex
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10Other works algorithmically related by OpenAlex
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| publication_date | 2025-08-06 |
| publication_year | 2025 |
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