Apoptosis-antagonizing transcription factor

Apoptosis antagonizing transcription factor
Identifiers
Symbols	AATF ; BFR2; CHE-1; CHE1; DED
External IDs	OMIM: 608463 MGI: 1929608 HomoloGene: 40811 GeneCards: AATF Gene
Gene ontology Molecular function • transcription factor activity, sequence-specific DNA binding • protein binding • leucine zipper domain binding • poly(A) RNA binding • tau protein binding Cellular component • nucleus • nucleolus • cytoplasm • Golgi apparatus • centrosome • focal adhesion Biological process • cellular response to DNA damage stimulus • cell adhesion • regulation of mitotic cell cycle • negative regulation of superoxide anion generation • embryonic cleavage • ribosome biogenesis • negative regulation of amyloid precursor protein biosynthetic process • positive regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of transcription from RNA polymerase II promoter • neurotrophin TRK receptor signaling pathway • apoptotic signaling pathway • negative regulation of reactive oxygen species metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	26574	56321
Ensembl	ENSG00000275700	ENSMUSG00000018697
UniProt	Q9NY61	Q9JKX4
RefSeq (mRNA)	NM_012138	NM_019816
RefSeq (protein)	NP_036270	NP_062790
Location (UCSC)	Chr 17: 36.95 – 37.06 Mb	Chr 11: 84.42 – 84.51 Mb
PubMed search

Protein AATF is a protein that in humans is encoded by the AATF gene.^[1][2][3]

Function

The protein encoded by this gene was identified on the basis of its interaction with MAP3K12/DLK, a protein kinase known to be involved in the induction of cell apoptosis. This gene product contains a leucine zipper, which is a characteristic motif of transcription factors, and was shown to exhibit strong transactivation activity when fused to Gal4 DNA binding domain. Overexpression of this gene interfered with MAP3K12 induced apoptosis.^[3]

Interactions

Apoptosis-antagonizing transcription factor has been shown to interact with:

• PAWR,^[4]
• POLR2J,^[2]
• Retinoblastoma protein,^[2][5] and
• Sp1 transcription factor.^[6]

References

1. Lindfors K, Halttunen T, Huotari P, Nupponen N, Vihinen M, Visakorpi T, Mäki M, Kainulainen H (Sep 2000). "Identification of novel transcription factor-like gene from human intestinal cells". Biochemical and Biophysical Research Communications 276 (2): 660–6. doi:10.1006/bbrc.2000.3480. PMID 11027528.
2. Fanciulli M, Bruno T, Di Padova M, De Angelis R, Iezzi S, Iacobini C, Floridi A, Passananti C (May 2000). "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb". FASEB Journal 14 (7): 904–12. PMID 10783144.
3. "Entrez Gene: AATF apoptosis antagonizing transcription factor".
4. Guo Q, Xie J (Feb 2004). "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4". The Journal of Biological Chemistry 279 (6): 4596–603. doi:10.1074/jbc.M309811200. PMID 14627703.
5. Bruno T, De Angelis R, De Nicola F, Barbato C, Di Padova M, Corbi N, Libri V, Benassi B, Mattei E, Chersi A, Soddu S, Floridi A, Passananti C, Fanciulli M (Nov 2002). "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb". Cancer Cell 2 (5): 387–99. doi:10.1016/s1535-6108(02)00182-4. PMID 12450794.
6. Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M (Sep 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.

Further reading

• Page G, Lödige I, Kögel D, Scheidtmann KH (Nov 1999). "AATF, a novel transcription factor that interacts with Dlk/ZIP kinase and interferes with apoptosis". FEBS Letters 462 (1-2): 187–91. doi:10.1016/S0014-5793(99)01529-X. PMID 10580117.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). "Directed proteomic analysis of the human nucleolus". Current Biology 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Scherl A, Couté Y, Déon C, Callé A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ (Nov 2002). "Functional proteomic analysis of human nucleolus". Molecular Biology of the Cell 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC 133617. PMID 12429849.
• Bruno T, De Angelis R, De Nicola F, Barbato C, Di Padova M, Corbi N, Libri V, Benassi B, Mattei E, Chersi A, Soddu S, Floridi A, Passananti C, Fanciulli M (Nov 2002). "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb". Cancer Cell 2 (5): 387–99. doi:10.1016/S1535-6108(02)00182-4. PMID 12450794.
• Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M (Sep 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.
• Guo Q, Xie J (Feb 2004). "AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4". The Journal of Biological Chemistry 279 (6): 4596–603. doi:10.1074/jbc.M309811200. PMID 14627703.
• Barbato C, Corbi N, Canu N, Fanciulli M, Serafino A, Ciotti M, Libri V, Bruno T, Amadoro G, De Angelis R, Calissano P, Passananti C (Dec 2003). "Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. Modulation during neuronal apoptosis". Molecular and Cellular Neurosciences 24 (4): 1038–50. doi:10.1016/j.mcn.2003.08.002. PMID 14697667.
• Burgdorf S, Leister P, Scheidtmann KH (Apr 2004). "TSG101 interacts with apoptosis-antagonizing transcription factor and enhances androgen receptor-mediated transcription by promoting its monoubiquitination". The Journal of Biological Chemistry 279 (17): 17524–34. doi:10.1074/jbc.M313703200. PMID 14761944.
• Xie J, Guo Q (Jun 2004). "AATF protects neural cells against oxidative damage induced by amyloid beta-peptide". Neurobiology of Disease 16 (1): 150–7. doi:10.1016/j.nbd.2004.02.003. PMID 15207272.
• Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (Apr 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Kaul D, Mehrotra A (Mar 2007). "Functional characterization of AATF transcriptome in human leukemic cells". Molecular and Cellular Biochemistry 297 (1-2): 215–20. doi:10.1007/s11010-006-9317-1. PMID 17006618.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.

External links

• AATF protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
• AATF human gene location in the UCSC Genome Browser.
• AATF human gene details in the UCSC Genome Browser.

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