Biology:Zinc finger and BTB domain-containing protein 16

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Short description: Protein found in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Zinc finger and BTB domain-containing protein 16 is a protein that in humans is encoded by the ZBTB16 gene.

Function

This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase. Specific instances of aberrant gene rearrangement at this locus have been associated with acute promyelocytic leukemia (APL)[1] and physiological roles have been identified in mouse Natural Killer T cells[2][3] and gamma-delta T cells.[4] Alternate transcriptional splice variants have been characterized in human.[5][6]

Interactions

Zinc finger and BTB domain-containing protein 16 has been shown to interact with:

See also

References

  1. ↑ "Fusion between a novel Krüppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia". The EMBO Journal 12 (3): 1161–7. 1993. doi:10.1002/j.1460-2075.1993.tb05757.x. PMID 8384553. 
  2. ↑ "The BTB-zinc finger transcriptional regulator, PLZF, controls the development of iNKT cell effector functions". Nature Immunology 9 (9): 1055–64. 2008. doi:10.1038/ni.1641. PMID 18660811. 
  3. ↑ "The transcription factor PLZF (Zbtb16) directs the effector program of the NKT cell lineage". Immunity 29 (3): 391–403. 2008. doi:10.1016/j.immuni.2008.07.011. PMID 18703361. 
  4. ↑ "TCR-inducible PLZF transcription factor required for innate phenotype of a subset of γδ T cells with restricted TCR diversity". Proceedings of the National Academy of Sciences of the United States of America 106 (30): 12453–8. 2009. doi:10.1073/pnas.0903895106. PMID 19617548. Bibcode: 2009PNAS..10612453K. 
  5. ↑ "Genomic sequence, structural organization, molecular evolution, and aberrant rearrangement of promyelocytic leukemia zinc finger gene". Proceedings of the National Academy of Sciences of the United States of America 96 (20): 11422–7. 1999. doi:10.1073/pnas.96.20.11422. PMID 10500192. Bibcode: 1999PNAS...9611422Z. 
  6. ↑ "ZBTB16 zinc finger and BTB domain containing 16". Entrez. 4 October 2009. https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7704. 
  7. ↑ "A novel angiotensin II type 2 receptor signaling pathway: possible role in cardiac hypertrophy". EMBO J. 22 (24): 6471–82. 2003. doi:10.1093/emboj/cdg637. PMID 14657020. 
  8. ↑ "Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF". Oncogene 19 (54): 6240–50. 2000. doi:10.1038/sj.onc.1203976. PMID 11175338. 
  9. ↑ "Plzf mediates transcriptional repression of HoxD gene expression through chromatin remodeling". Dev. Cell 3 (4): 499–510. 2002. doi:10.1016/s1534-5807(02)00289-7. PMID 12408802. 
  10. ↑ 10.0 10.1 "The acute promyelocytic leukemia-associated protein, promyelocytic leukemia zinc finger, regulates 1,25-dihydroxyvitamin D(3)-induced monocytic differentiation of U937 cells through a physical interaction with vitamin D(3) receptor". Blood 98 (12): 3290–300. 2001. doi:10.1182/blood.v98.12.3290. PMID 11719366. 
  11. ↑ "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Res. 62 (23): 7050–8. 2002. PMID 12460926. 
  12. ↑ "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. 277 (40): 37045–53. 2002. doi:10.1074/jbc.M203336200. PMID 12145280. 
  13. ↑ "PLZF induces megakaryocytic development, activates Tpo receptor expression and interacts with GATA1 protein". Oncogene 21 (43): 6669–79. 2002. doi:10.1038/sj.onc.1205884. PMID 12242665. 
  14. ↑ "Interactions of GATA-2 with the promyelocytic leukemia zinc finger (PLZF) protein, its homologue FAZF, and the t(11;17)-generated PLZF-retinoic acid receptor alpha oncoprotein". Blood 99 (9): 3404–10. 2002. doi:10.1182/blood.v99.9.3404. PMID 11964310. 
  15. ↑ 15.0 15.1 15.2 15.3 "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene 23 (54): 8777–84. 2004. doi:10.1038/sj.onc.1208128. PMID 15467736. 
  16. ↑ 16.0 16.1 16.2 "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene 16 (19): 2549–56. 1998. doi:10.1038/sj.onc.1202043. PMID 9627120. 
  17. ↑ 17.0 17.1 17.2 "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". J. Biol. Chem. 273 (42): 27695–702. 1998. doi:10.1074/jbc.273.42.27695. PMID 9765306. 
  18. ↑ 18.0 18.1 "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. 277 (24): 22045–52. 2002. doi:10.1074/jbc.M201736200. PMID 11929873. https://hal.archives-ouvertes.fr/hal-00379714/file/Lemercier_BCL6_JBC_2002._doc.pdf. 
  19. ↑ "Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF". J. Cell Biol. 163 (3): 489–502. 2003. doi:10.1083/jcb.200303017. PMID 14597771. 
  20. ↑ "Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF". Biochem. Biophys. Res. Commun. 320 (2): 376–82. 2004. doi:10.1016/j.bbrc.2004.05.176. PMID 15219838. 
  21. ↑ "The Flt3 internal tandem duplication mutant inhibits the function of transcriptional repressors by blocking interactions with SMRT". Blood 103 (12): 4650–8. 2004. doi:10.1182/blood-2003-08-2759. PMID 14982881. 
  22. ↑ "SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 9028–33. 1997. doi:10.1073/pnas.94.17.9028. PMID 9256429. Bibcode: 1997PNAS...94.9028H. 
  23. ↑ "Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proc. Natl. Acad. Sci. U.S.A. 94 (19): 10255–60. 1997. doi:10.1073/pnas.94.19.10255. PMID 9294197. Bibcode: 1997PNAS...9410255K. 
  24. ↑ "The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein". Mol. Cell. Biol. 20 (6): 2075–86. 2000. doi:10.1128/mcb.20.6.2075-2086.2000. PMID 10688654. 
  25. ↑ "AML-1/ETO fusion protein is a dominant negative inhibitor of transcriptional repression by the promyelocytic leukemia zinc finger protein". Blood 96 (12): 3939–47. 2000. doi:10.1182/blood.V96.12.3939. PMID 11090081. 
  26. ↑ "PLZF is a negative regulator of retinoic acid receptor transcriptional activity". Nucl. Recept. 1 (1): 6. 2003. doi:10.1186/1478-1336-1-6. PMID 14521715. 
  27. ↑ "A novel BTB/POZ transcriptional repressor protein interacts with the Fanconi anemia group C protein and PLZF". Blood 94 (11): 3737–47. 1999. doi:10.1182/blood.V94.11.3737. PMID 10572087. 

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.