Abstract 1729 Mllt1, an epigenetic reader protein, is required to maintain B-lymphopoiesis

MLLT1 (aka ENL) is an epigenetic reader protein that binds to crotonylated/acetylated lysine residues of histone 3 through its N-terminal YEATS domain. Multiple different positive and negative regulatory complexes compete for binding to the MLLT1 C-terminal domain. MLLT1 was initially identified as a chromosomal translocation partner to MLL in a class of MLL-rearranged leukemias. MLL-ENL fusion protein is known to cause both lymphoid (predominantly B-ALL) and mixed lineage leukemias. MLLT1 has been implicated in leukemic stem cell survival in MLL-rearranged cell lines but its role in normal hematopoiesis has not been investigated.

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Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109253
Primary Topic
Epigenetics and DNA Methylation
Type
article
Field-Weighted Citation Impact
0.00

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Abstract 1729 Mllt1, an epigenetic reader protein, is required to maintain B-lymphopoiesis

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Abstract 1729 Mllt1, an epigenetic reader protein, is required to maintain B-lymphopoiesis

Janani Prakash, Shubin Zhang, Charles S. Hemenway, Nicholas J. Achille, Nancy J. Zeleznik‐Le
article en

Abstract

MLLT1 (aka ENL) is an epigenetic reader protein that binds to crotonylated/acetylated lysine residues of histone 3 through its N-terminal YEATS domain. Multiple different positive and negative regulatory complexes compete for binding to the MLLT1 C-terminal domain. MLLT1 was initially identified as a chromosomal translocation partner to MLL in a class of MLL-rearranged leukemias. MLL-ENL fusion protein is known to cause both lymphoid (predominantly B-ALL) and mixed lineage leukemias. MLLT1 has been implicated in leukemic stem cell survival in MLL-rearranged cell lines but its role in normal hematopoiesis has not been investigated.

Journal of Biological ChemistryVol. 301(5)
Loyola University Chicago (US)
National Cancer Institute
Zero hunger
Openalex Percentile: Top 88%
Epigenetics and DNA Methylation
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