LMO2

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Protein-coding gene in the species Homo sapiens

title: "LMO2" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/LMO2" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

LIM domain only 2 (rhombotin-like 1), also known as LMO2, RBTNL1, RBTN2, RHOM2, LIM Domain Only Protein 2, TTG2, and T-Cell Translocation Protein 2, is a protein which in humans is encoded by the LMO2 gene.

Structure

LMO2 is characterized as a small, cysteine-rich protein comprising two tandem LIM domains. Each LIM domain features a conserved double zinc finger motif, wherein zinc ions are coordinated by cysteine and histidine residues. These domains are critical for LMO2's primary function as a scaffolding protein facilitating protein-protein interactions within transcriptional regulatory complexes. Notably, LMO2 lacks an intrinsic DNA-binding domain; its influence on gene expression is mediated through its recruitment into multi-protein assemblies. The inter-domain linker region contributes to the protein's overall conformational dynamics, potentially modulating its interaction with diverse binding partners. The structural integrity conferred by the zinc fingers within the LIM domains is essential for maintaining the protein's functional architecture in the context of hematopoiesis and leukemogenesis.

Function

LMO2 encodes a cysteine-rich, two LIM domain protein that is required for yolk sac erythropoiesis. The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved.

Clinical significance

Aberrant LMO2 expression is a significant feature of T cell acute lymphoblastic leukaemia with multiple described mechanisms of activation. The LMO2 transcription start site is located approximately 25 kb downstream from the 11p13 T-cell translocation cluster (11p13 ttc), where a number of T-cell acute lymphoblastic leukemia-specific translocations occur. An upstream noncoding DNA element is also the site of recurrent mutations in T cell acute lymphoblastic leukaemia, leading the recruitment of the transcription factor MYB and significant H3K27ac enrichment and thus the formation of an aberrant enhancer which up-regulates the expression of LMO2 Furthermore, recurrent and somatically acquired mutations of LMO2 intron 1 lead to its over-expression in both adult and paediatric T cell acute lymphoblastic leukaemia. These mutations introduce new transcription factor binding sites for MYB, ETS1 and RUNX1 allowing for the formation of an aberrant promoter which drives LMO2 expression.

Interactions

LMO2 has been shown to interact with:

References

References

  1. (May 1991). "The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13". Proceedings of the National Academy of Sciences of the United States of America.
  2. (February 2011). "Structure of the leukemia oncogene LMO2: implications for the assembly of a hematopoietic transcription factor complex". Blood.
  3. (July 1994). "The oncogenic cysteine-rich LIM domain protein rbtn2 is essential for erythroid development". Cell.
  4. (December 1992). "T-cell acute lymphoblastic lymphoma induced in transgenic mice by the RBTN1 and RBTN2 LIM-domain genes". Oncogene.
  5. {{EntrezGene. 4005
  6. (February 2017). "Small genomic insertions form enhancers that misregulate oncogenes". Nature Communications.
  7. (June 2017). "Activation of the ''LMO2'' oncogene through a somatically acquired neomorphic promoter in T-cell acute lymphoblastic leukemia". Blood.
  8. (October 1995). "Association of erythroid transcription factors: complexes involving the LIM protein RBTN2 and the zinc-finger protein GATA1". Proceedings of the National Academy of Sciences of the United States of America.
  9. (April 1997). "T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2". Oncogene.
  10. (June 2002). "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Letters.
  11. (October 1994). "Specific in vivo association between the bHLH and LIM proteins implicated in human T cell leukemia". The EMBO Journal.
  12. (August 1994). "The LIM protein RBTN2 and the basic helix-loop-helix protein TAL1 are present in a complex in erythroid cells". Proceedings of the National Academy of Sciences of the United States of America.
  13. (January 2006). "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". The EMBO Journal.

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