anti-Myocyte Enhancer Factor 2B (MEF2B) Antikörper

Zebrafish Myocyte Enhancer Factor 2B (MEF2B) Interaktionspartner

1. Mef2 controls skeletal muscle formation after terminal differentiation.

Mouse (Murine) Myocyte Enhancer Factor 2B (MEF2B) Interaktionspartner

1. Mef2b deletion reduces germinal center (GC) formation in mice and identify MEF2B transcriptional targets in GC, with roles in cell proliferation, apoptosis, GC confinement, and differentiation. The most common lymphoma-associated MEF2B mutant (MEF2BD83V) is hypomorphic yet escapes binding and negative regulation by components of the HUCA complex and class IIa HDACs.

2. Whereas MEF2A is absolutely required for proper myoblast differentiation, MEF2B, -C, and -D were found to be dispensable for this process.

3. Calcineurein regulates skeletal muscle differentiation by activating MEF2 and MyoD transcription factors.

4. Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo

Human Myocyte Enhancer Factor 2B (MEF2B) Interaktionspartner

1. Studied expression of myocyte enhancer factor 2B (MEF2B) as part of the diffuse large (DLBCL) B-cell lymphoma 6 (BCL6) transcription complex in diffuse large B-cell lymphoma tissue samples and cell lines. Findings indicate MEF2B to be an essential component of the BCL6 gene transcriptional complex for the regulation of DLBCL growth thru promotion of BCL6 expression.

2. Mef2b deletion reduces germinal center (GC) formation in mice and identify MEF2B transcriptional targets in GC, with roles in cell proliferation, apoptosis, GC confinement, and differentiation. The most common lymphoma-associated MEF2B mutant (MEF2BD83V) is hypomorphic yet escapes binding and negative regulation by components of the HUCA complex and class IIa HDACs.

3. Although the mechanisms by which the D83V mutation in MEF2B promote oncogenesis in lymphoma cells remain to be elucidated, the observation that a mutation hotspot coincides with a conformation switch site on MEF2B reflects a remarkable convergence of tumor growth selection pressure and the physical/ chemical forces behind protein folding.

4. The Apo structure of MEF2B reveals a largely preformed DNA binding interface that may be important for recognizing the shape of DNA from the minor groove side.

5. MEF2B shows superior sensitivity and specificity than LMO2 and HGAL in the differential diagnosis of follicular lymphoma versus marginal zone lymphoma and is particularly useful in FL with plasmacytoid differentiation, which may have morphologic and immunophenotypic overlap with MZL.

6. Expression of J chain immunoglobulin and MEF2B are useful in differentiating classical Hodgkin lymphoma from nodular lymphocyte predominant Hodgkin lymphoma and primary mediastinal large B-cell lymphoma.

7. K4E, Y69H and D83V mutations decrease the capacity of MEF2B to activate transcription and decrease its effects on cell migration.

8. Epstein-Barr Virus EBNA1 bound to host genes of high significance for B-cell growth and function, including MEF2B, IL6R, and EBF1.

9. We conclude that MEF2B is a valuable marker of normal germinal center B cells, potentially useful in differential diagnosis of small B cell lymphomas.

10. MEF2B mutations lead to deregulated expression of the oncogene BCL6 in diffuse large B cell lymphoma.

11. MEF2B has a role in myogenic transformation of the epithelial to a myofibroblast phenotype

12. The phylogenetic tree result shows that MEF2B may be original because of its difference of sequences and evolutional relation.

13. 32% of diffuse large B-cell lymphoma and 89% of follicular lymphoma cases had somatic mutations in MLL2, and 11.4% and 13.4% of DLBCL and FL cases, respectively, had mutations in MEF2B

14. Crystal structure of the MADS-box/MEF2S domain of human MEF2B bound to a motif of the transcriptional co-repressor Cabin1 and DNA at 2.2 A resolution

15. myogenin and myocyte enhancer factor-2 expression are triggered by membrane hyperpolarization during human myoblast differentiation

16. The crystal structure of a histone deacetylase 9 (HDAC9)/myocyte enhancer factor-2 (MEF2)/DNA complex reveals that HDAC9 binds to a hydrophobic groove of the MEF2 dimer.

17. Study demonstrates that human intestinal cell BCMO1 expression is dependent on the functional cooperation between peroxisome proliferator-activated receptor-gamma and myocyte enhancer factor 2 isoforms.

18. MEF2 proteins are an important component in Galpha13-mediated angiogenesis.

Cow (Bovine) Myocyte Enhancer Factor 2B (MEF2B) Interaktionspartner

1. This study provides new evidence of the significant role played by Mef2B in the postnatal muscle growth and development in cattle, and indicates that Mef2B can be a promising molecular marker for carcass quality-related traits in adult cattle.