Zinc finger and BTB domain-containing protein 16

Last updated
ZBTB16
Protein ZBTB16 PDB 1buo.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ZBTB16 , PLZF, ZNF145, zinc finger and BTB domain containing 16
External IDs OMIM: 176797 MGI: 103222 HomoloGene: 21214 GeneCards: ZBTB16
Orthologs
SpeciesHumanMouse
Entrez

7704

235320

Ensembl

ENSG00000109906

ENSMUSG00000066687

UniProt

Q05516

Q3UQ17

RefSeq (mRNA)

NM_001018011
NM_006006
NM_001354750
NM_001354751
NM_001354752

Contents

NM_001033324
NM_001364543

RefSeq (protein)

NP_001018011
NP_005997
NP_001341679
NP_001341680
NP_001341681

NP_001028496
NP_001351472

Location (UCSC) Chr 11: 114.06 – 114.26 Mb Chr 9: 48.57 – 48.75 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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) [5] and physiological roles have been identified in mouse Natural Killer T cells [6] [7] and gamma-delta T cells. [8] Alternate transcriptional splice variants have been characterized in human. [9] [10]

Interactions

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

See also

Related Research Articles

<span class="mw-page-title-main">Acute promyelocytic leukemia</span> Subtype of acute myeloid leukaemia characterised by accumulation of promyelocytes

Acute promyelocytic leukemia is a subtype of acute myeloid leukemia (AML), a cancer of the white blood cells. In APL, there is an abnormal accumulation of immature granulocytes called promyelocytes. The disease is characterized by a chromosomal translocation involving the retinoic acid receptor alpha (RARA) gene and is distinguished from other forms of AML by its responsiveness to all-trans retinoic acid therapy. Acute promyelocytic leukemia was first characterized in 1957 by French and Norwegian physicians as a hyperacute fatal illness, with a median survival time of less than a week. Today, prognoses have drastically improved; 10-year survival rates are estimated to be approximately 80-90% according to one study.

<span class="mw-page-title-main">GATA1</span> Protein-coding gene in humans

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<span class="mw-page-title-main">Nuclear receptor co-repressor 1</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor co-repressor 1 also known as thyroid-hormone- and retinoic-acid-receptor-associated co-repressor 1 (TRAC-1) is a protein that in humans is encoded by the NCOR1 gene.

<span class="mw-page-title-main">Nuclear receptor co-repressor 2</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor co-repressor 2 (NCOR2) is a transcriptional coregulatory protein that contains several nuclear receptor-interacting domains. In addition, NCOR2 appears to recruit histone deacetylases to DNA promoter regions. Hence NCOR2 assists nuclear receptors in the down regulation of target gene expression. NCOR2 is also referred to as a silencing mediator for retinoid or thyroid-hormone receptors (SMRT) or T3 receptor-associating cofactor 1 (TRAC-1).

<span class="mw-page-title-main">Corepressor</span> Molecule that represses the expression of genes

In genetics and molecular biology, a corepressor is a molecule that represses the expression of genes. In prokaryotes, corepressors are small molecules whereas in eukaryotes, corepressors are proteins. A corepressor does not directly bind to DNA, but instead indirectly regulates gene expression by binding to repressors.

<span class="mw-page-title-main">Promyelocytic leukemia protein</span> Protein-coding gene in the species Homo sapiens

Promyelocytic leukemia protein (PML) is the protein product of the PML gene. PML protein is a tumor suppressor protein required for the assembly of a number of nuclear structures, called PML-nuclear bodies, which form amongst the chromatin of the cell nucleus. These nuclear bodies are present in mammalian nuclei, at about 1 to 30 per cell nucleus. PML-NBs are known to have a number of regulatory cellular functions, including involvement in programmed cell death, genome stability, antiviral effects and controlling cell division. PML mutation or loss, and the subsequent dysregulation of these processes, has been implicated in a variety of cancers.

<span class="mw-page-title-main">Wilms tumor protein</span> Transcription factor gene involved in the urogenital system

Wilms tumor protein (WT33) is a protein that in humans is encoded by the WT1 gene on chromosome 11p.

<span class="mw-page-title-main">BCL6</span> Transcription factor for converting Naive T cells to TFH

Bcl-6 is a protein that in humans is encoded by the BCL6 gene. BCL6 is a master transcription factor for regulation of T follicular helper cells proliferation. BCL6 has three evolutionary conserved structural domains. The interaction of these domains with corepressors allows for germinal center development and leads to B cell proliferation.

<span class="mw-page-title-main">Retinoic acid receptor alpha</span> Protein-coding gene in the species Homo sapiens

Retinoic acid receptor alpha (RAR-α), also known as NR1B1 is a nuclear receptor that in humans is encoded by the RARA gene.

<span class="mw-page-title-main">SIN3A</span> Protein-coding gene in the species Homo sapiens

Paired amphipathic helix protein Sin3a is a protein that in humans is encoded by the SIN3A gene.

<span class="mw-page-title-main">GATA2</span> Protein-coding gene in the species Homo sapiens

GATA2 or GATA-binding factor 2 is a transcription factor, i.e. a nuclear protein which regulates the expression of genes. It regulates many genes that are critical for the embryonic development, self-renewal, maintenance, and functionality of blood-forming, lympathic system-forming, and other tissue-forming stem cells. GATA2 is encoded by the GATA2 gene, a gene which often suffers germline and somatic mutations which lead to a wide range of familial and sporadic diseases, respectively. The gene and its product are targets for the treatment of these diseases.

<span class="mw-page-title-main">RUNX1T1</span> Protein-coding gene in humans

Protein CBFA2T1 is a protein that in humans is encoded by the RUNX1T1 gene.

<span class="mw-page-title-main">MECOM</span> Protein-coding gene in the species Homo sapiens

MDS1 and EVI1 complex locus protein EVI1 (MECOM) also known as ecotropic virus integration site 1 protein homolog (EVI-1) or positive regulatory domain zinc finger protein 3 (PRDM3) is a protein that in humans is encoded by the MECOM gene. EVI1 was first identified as a common retroviral integration site in AKXD murine myeloid tumors. It has since been identified in a plethora of other organisms, and seems to play a relatively conserved developmental role in embryogenesis. EVI1 is a nuclear transcription factor involved in many signaling pathways for both coexpression and coactivation of cell cycle genes.

<span class="mw-page-title-main">FIP1L1</span> Protein-coding gene in the species Homo sapiens

Factor interacting with PAPOLA and CPSF1 is a protein that in humans is encoded by the FIP1L1 gene. A medically important aspect of the FIP1L1 gene is its fusion with other genes to form fusion genes which cause clonal hypereosinophilia and leukemic diseases in humans.

<span class="mw-page-title-main">SIN3B</span> Protein-coding gene in the species Homo sapiens

Paired amphipathic helix protein Sin3b is a protein that in humans is encoded by the SIN3B gene.

<span class="mw-page-title-main">PRAM1</span> Protein-coding gene in the species Homo sapiens

PML-RARA-regulated adapter molecule 1 is a protein that in humans is encoded by the PRAM1 gene.

<span class="mw-page-title-main">ZBTB32</span> Protein-coding gene in the species Homo sapiens

Zinc finger and BTB domain-containing protein 32 is a protein that in humans is encoded by the 1960 bp ZBTB32 gene. The 52 kDa protein is a transcriptional repressor and the gene is expressed in T and B cells upon activation, but also significantly in testis cells. It is a member of the Poxviruses and Zinc-finger (POZ) and Krüppel (POK) family of proteins, and was identified in multiple screens involving either immune cell tumorigenesis or immune cell development.

<span class="mw-page-title-main">BTB/POZ domain</span>

The BTB/POZ domain is a structural domain found in proteins across the domain Eukarya. Given its prevalence in eukaryotes and its absence in Archaea and bacteria, it likely arose after the origin of eukaryotes. While primarily a protein-protein interaction domain, some BTB domains have additional functionality in transcriptional regulation, cytoskeletal mobility, protein ubiquitination and degradation, and ion channel formation and operation. BTB domains have traditionally been classified by the other structural features present in the protein.

<span class="mw-page-title-main">MYND zinc finger</span>

In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repression is believed to be a general mechanism of leukemogenesis caused by the t(8;21) translocations that fuse ETO with the acute myelogenous leukemia 1 (AML1) protein. ETO has been shown to be a co-repressor recruited by the promyelocytic leukemia zinc finger (PLZF) protein. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression. The current evidence suggests that the MYND motif in mammalian proteins constitutes a protein-protein interaction domain that functions as a co-repressor-recruiting interface.

The RARA gene, also known as NR1B1, is a protein coding gene located on chromosome 17 that provides the instructions required to make transcription factor Retinoic Acid Receptor Alpha.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000109906 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000066687 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Chen Z, Brand NJ, Chen A, Chen SJ, Tong JH, Wang ZY, Waxman S, Zelent A (1993). "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. doi:10.1002/j.1460-2075.1993.tb05757.x. PMC   413318 . PMID   8384553.
  6. ↑ Kovalovsky D, Uche OU, Eladad S, Hobbs RM, Yi W, Alonzo E, Chua K, Eidson M, et al. (2008). "The BTB-zinc finger transcriptional regulator, PLZF, controls the development of iNKT cell effector functions". Nature Immunology. 9 (9): 1055–64. doi:10.1038/ni.1641. PMC   2662733 . PMID   18660811.
  7. ↑ Savage AK, Constantinides MG, Han J, Picard D, Martin E, Li B, Lantz O, Bendelac A (2008). "The transcription factor PLZF (Zbtb16) directs the effector program of the NKT cell lineage". Immunity. 29 (3): 391–403. doi:10.1016/j.immuni.2008.07.011. PMC   2613001 . PMID   18703361.
  8. ↑ Kreslavsky T, Savage AK, Hobbs R, Gounari F, Bronson R, Pereira P, Pandolfi PP, Bendelac A, von Boehmer H (2009). "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. Bibcode:2009PNAS..10612453K. doi: 10.1073/pnas.0903895106 . PMC   2718370 . PMID   19617548.
  9. ↑ Zhang T, Xiong H, Kan LX, Zhang CK, Jiao XF, Fu G, Zhang QH, Lu L, et al. (1999). "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. Bibcode:1999PNAS...9611422Z. doi: 10.1073/pnas.96.20.11422 . PMC   18049 . PMID   10500192.
  10. ↑ "ZBTB16 zinc finger and BTB domain containing 16". Entrez . 4 October 2009. Retrieved 10 October 2009.
  11. ↑ Senbonmatsu T, Saito T, Landon EJ, Watanabe O, Price E, Roberts RL, Imboden H, Fitzgerald TG, et al. (2003). "A novel angiotensin II type 2 receptor signaling pathway: possible role in cardiac hypertrophy". EMBO J. 22 (24): 6471–82. doi:10.1093/emboj/cdg637. PMC   291832 . PMID   14657020.
  12. ↑ Dhordain P, Albagli O, Honore N, Guidez F, Lantoine D, Schmid M, The HD, Zelent A, Koken MH (2000). "Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF". Oncogene. 19 (54): 6240–50. doi:10.1038/sj.onc.1203976. PMID   11175338. S2CID   23619694.
  13. ↑ Barna M, Merghoub T, Costoya JA, Ruggero D, Branford M, Bergia A, Samori B, Pandolfi PP (2002). "Plzf mediates transcriptional repression of HoxD gene expression through chromatin remodeling". Dev. Cell. 3 (4): 499–510. doi: 10.1016/s1534-5807(02)00289-7 . PMID   12408802.
  14. 1 2 Ward JO, McConnell MJ, Carlile GW, Pandolfi PP, Licht JD, Freedman LP (2001). "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. doi: 10.1182/blood.v98.12.3290 . PMID   11719366.
  15. ↑ Puccetti E, Obradovic D, Beissert T, Bianchini A, Washburn B, Chiaradonna F, Boehrer S, Hoelzer D, et al. (2002). "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer Res. 62 (23): 7050–8. PMID   12460926.
  16. ↑ McLoughlin P, Ehler E, Carlile G, Licht JD, Schäfer BW (2002). "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. doi: 10.1074/jbc.M203336200 . PMID   12145280.
  17. ↑ Labbaye C, Quaranta MT, Pagliuca A, Militi S, Licht JD, Testa U, Peschle C (2002). "PLZF induces megakaryocytic development, activates Tpo receptor expression and interacts with GATA1 protein". Oncogene. 21 (43): 6669–79. doi: 10.1038/sj.onc.1205884 . PMID   12242665.
  18. ↑ Tsuzuki S, Enver T (2002). "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. doi: 10.1182/blood.v99.9.3404 . PMID   11964310.
  19. 1 2 3 4 Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A (2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene. 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID   15467736. S2CID   26092755.
  20. 1 2 3 David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID   9627120. S2CID   655636.
  21. 1 2 3 Wong CW, Privalsky ML (1998). "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. doi: 10.1074/jbc.273.42.27695 . PMID   9765306.
  22. 1 2 Lemercier C, Brocard MP, Puvion-Dutilleul F, Kao HY, Albagli O, Khochbin S (2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor" (PDF). J. Biol. Chem. 277 (24): 22045–52. doi: 10.1074/jbc.M201736200 . PMID   11929873. S2CID   19024903.
  23. ↑ Nanba D, Mammoto A, Hashimoto K, Higashiyama S (2003). "Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF". J. Cell Biol. 163 (3): 489–502. doi:10.1083/jcb.200303017. PMC   2173632 . PMID   14597771.
  24. ↑ Nanba D, Toki F, Higashiyama S (2004). "Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF". Biochem. Biophys. Res. Commun. 320 (2): 376–82. doi:10.1016/j.bbrc.2004.05.176. PMID   15219838.
  25. ↑ Takahashi S, McConnell MJ, Harigae H, Kaku M, Sasaki T, Melnick AM, Licht JD (2004). "The Flt3 internal tandem duplication mutant inhibits the function of transcriptional repressors by blocking interactions with SMRT". Blood. 103 (12): 4650–8. doi: 10.1182/blood-2003-08-2759 . PMID   14982881.
  26. ↑ Hong SH, David G, Wong CW, Dejean A, Privalsky ML (1997). "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. Bibcode:1997PNAS...94.9028H. doi: 10.1073/pnas.94.17.9028 . PMC   23013 . PMID   9256429.
  27. ↑ Koken MH, Reid A, Quignon F, Chelbi-Alix MK, Davies JM, Kabarowski JH, Zhu J, Dong S, et al. (1997). "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. Bibcode:1997PNAS...9410255K. doi: 10.1073/pnas.94.19.10255 . PMC   23349 . PMID   9294197.
  28. ↑ Melnick AM, Westendorf JJ, Polinger A, Carlile GW, Arai S, Ball HJ, Lutterbach B, Hiebert SW, Licht JD (2000). "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. doi:10.1128/mcb.20.6.2075-2086.2000. PMC   110824 . PMID   10688654.
  29. ↑ Melnick A, Carlile GW, McConnell MJ, Polinger A, Hiebert SW, Licht JD (2000). "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. doi:10.1182/blood.V96.12.3939. PMID   11090081.
  30. ↑ Martin PJ, Delmotte MH, Formstecher P, Lefebvre P (2003). "PLZF is a negative regulator of retinoic acid receptor transcriptional activity". Nucl. Recept. 1 (1): 6. doi: 10.1186/1478-1336-1-6 . PMC   212040 . PMID   14521715.
  31. ↑ Hoatlin ME, Zhi Y, Ball H, Silvey K, Melnick A, Stone S, Arai S, Hawe N, et al. (1999). "A novel BTB/POZ transcriptional repressor protein interacts with the Fanconi anemia group C protein and PLZF". Blood. 94 (11): 3737–47. doi:10.1182/blood.V94.11.3737. PMID   10572087.

Further reading

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