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Peregrin also known as bromodomain and PHD finger-containing protein 1 is a protein that in humans is encoded by the BRPF1 gene located on 3p26-p25. Peregrin is a multivalent chromatin regulator that recognizes different epigenetic marks and activates three histone acetyltransferases (Moz, Morf and Hbo1). BRPF1 contains two PHD fingers, one bromodomain and one chromo/Tudor-related Pro-Trp-Trp-Pro (PWWP) domain.
File:模式图1-01-01.tifBrpf1 forms a stable complex with Moz/Morf-Hbo1 and targets to chromatin to regulate transcription.[1]File:Brpf1 name.tifBrpf1 null mutant mouse dies at embryonic day 9.5.[2][3] Forebrain-specific knock out of Brpf1 cause hypoplasia in the dentate gyrus of mouse.[4]
Embryo development
Brpf1 gene is very conserved and has a critical role in different developmental processes.[1][2][3]Zebrafish BRPF1, which is coordinated by its particular set of PWWP domains, mediates Moz -dependent histone acetylation and maintains Hox genes expression throughout vertebrate development, hence determines the proper pharyngeal segmental identities.[5] Furthermore, Brpf1 may not only has significant role for maintaining the anterior-posterior axis of the craniofacial skeleton, but also the dorsal-ventral axis of the caudal skeleton.[6] Recent studies have shown that ablation of the mouse Brpf1 gene causes embryonic lethality at embryonic day 9.5.[2][3] Specifically, Brpf1 regulates placenta vascular formation, neural tube closure, primitive hematopoiesis and embryonic fibroblast proliferation.[2][3]
Recently, Brpf1 was reported to play the tumor suppressor or oncogenic role in several malignant tumors, including leukemia, medulloblastoma and endometrial stromal sarcoma.[1][8][9][10]Brpf1 was considered a tumor suppressor gene because mutations in cancer cells appear to diminish the function of Brpf1[8][9] However, oncogenic role of Brpf1 is also possible in cancer. For example, Brpf1 can form a stable complex with Moz-Tif2, which could lead to the development of human acute myeloid leukemia (AML).[10] There is another Brpf1 related complex Brpf1–Ing5–Eaf6, which also plays a direct role in cancer.[1]
↑ 1.01.11.21.3Yang XJ (2015). "MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease". Biochimica et Biophysica Acta. 1853 (8): 1818–26. doi:10.1016/j.bbamcr.2015.04.014. PMID25920810.
↑Hibiya K, Katsumoto T, Kondo T, Kitabayashi I, Kudo A (2009). "Brpf1, a subunit of the MOZ histone acetyl transferase complex, maintains expression of anterior and posterior Hox genes for proper patterning of craniofacial and caudal skeletons". Developmental Biology. 329 (2): 176–90. doi:10.1016/j.ydbio.2009.02.021. PMID19254709.
↑Yan K, You L, Degerny C, Ghorbani M, Liu X, Chen L, Li L, Miao D, Yang XJ (2016). "The Chromatin Regulator BRPF3 Preferentially Activates the HBO1 Acetyltransferase but Is Dispensable for Mouse Development and Survival". The Journal of Biological Chemistry. 291 (6): 2647–63. doi:10.1074/jbc.M115.703041. PMID26677226.
↑ 10.010.1Shima H, Yamagata K, Aikawa Y, Shino M, Koseki H, Shimada H, Kitabayashi I (2014). "Bromodomain-PHD finger protein 1 is critical for leukemogenesis associated with MOZ-TIF2 fusion". International Journal of Hematology. 99 (1): 21–31. doi:10.1007/s12185-013-1466-x. PMID24258712.
Mishima Y, Miyagi S, Saraya A, Negishi M, Endoh M, Endo TA, Toyoda T, Shinga J, Katsumoto T, Chiba T, Yamaguchi N, Kitabayashi I, Koseki H, Iwama A (Sep 2011). "The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14 and required for fetal liver erythropoiesis". Blood. 118 (9): 2443–53. doi:10.1182/blood-2011-01-331892. PMID21753189.
Vezzoli A, Bonadies N, Allen MD, Freund SM, Santiveri CM, Kvinlaug BT, Huntly BJ, Göttgens B, Bycroft M (May 2010). "Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1". Nature Structural & Molecular Biology. 17 (5): 617–9. doi:10.1038/nsmb.1797. PMID20400950.
Hibiya K, Katsumoto T, Kondo T, Kitabayashi I, Kudo A (May 2009). "Brpf1, a subunit of the MOZ histone acetyl transferase complex, maintains expression of anterior and posterior Hox genes for proper patterning of craniofacial and caudal skeletons". Developmental Biology. 329 (2): 176–90. doi:10.1016/j.ydbio.2009.02.021. PMID19254709.