ATF4: Difference between revisions
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== Function == | == Function == | ||
This gene encodes a [[transcription factor]] that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 ([[activating transcription factor 2|CREB-2]]). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the [[AP-1 (transcription factor)|AP-1]] family of transcription factors, cAMP-response element binding proteins ([[CREB]]s) and CREB-like proteins. These transcription factors share a [[leucine zipper]] region that is involved in protein–protein interactions, located [[C-terminus|C-terminal]] to a stretch of basic amino acids that functions as a [[DNA-binding domain]]. Two alternative transcripts encoding the same protein have been described. Two [[pseudogene]]s are located on the X chromosome at q28 in a region containing a large inverted duplication.<ref name="entrez">{{cite web | title = Entrez Gene: ATF4 activating transcription factor 4 (tax-responsive enhancer element B67)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=468| | This gene encodes a [[transcription factor]] that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 ([[activating transcription factor 2|CREB-2]]). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the [[AP-1 (transcription factor)|AP-1]] family of transcription factors, cAMP-response element binding proteins ([[CREB]]s) and CREB-like proteins. These transcription factors share a [[leucine zipper]] region that is involved in protein–protein interactions, located [[C-terminus|C-terminal]] to a stretch of basic amino acids that functions as a [[DNA-binding domain]]. Two alternative transcripts encoding the same protein have been described. Two [[pseudogene]]s are located on the X chromosome at q28 in a region containing a large inverted duplication.<ref name="entrez">{{cite web | title = Entrez Gene: ATF4 activating transcription factor 4 (tax-responsive enhancer element B67)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=468| access-date = }}</ref> | ||
ATF4 transcription factor is also known to play role in [[osteoblast]] differentiation along with [[RUNX2]] and [[Sp7 transcription factor|osterix]].<ref name="pmid18728356">{{cite journal | vauthors = Franceschi RT, Ge C, Xiao G, Roca H, Jiang D | title = Transcriptional regulation of osteoblasts | journal = Cells | ATF4 transcription factor is also known to play role in [[osteoblast]] differentiation along with [[RUNX2]] and [[Sp7 transcription factor|osterix]].<ref name="pmid18728356">{{cite journal | vauthors = Franceschi RT, Ge C, Xiao G, Roca H, Jiang D | title = Transcriptional regulation of osteoblasts | journal = Cells Tissues Organs | volume = 189 | issue = 1-4 | pages = 144–52 | year = 2009 | pmid = 18728356 | pmc = 3512205 | doi = 10.1159/000151747 }}</ref> Terminal osteoblast differentiation, represented by matrix mineralization, is significantly inhibited by the inactivation of [[c-Jun N-terminal kinases|JNK]]. JNK inactivation downregulates expression of ATF-4 and, subsequently, matrix mineralization.<ref name="pmid19016586">{{cite journal | vauthors = Matsuguchi T, Chiba N, Bandow K, Kakimoto K, Masuda A, Ohnishi T | title = JNK activity is essential for Atf4 expression and late-stage osteoblast differentiation | journal = Journal of Bone and Mineral Research | volume = 24 | issue = 3 | pages = 398–410 | date = March 2009 | pmid = 19016586 | doi = 10.1359/jbmr.081107 }}</ref> IMPACT protein regulates ATF4 in C. elegans to promote lifespan.<ref>{{cite journal | vauthors = Ferraz RC, Camara H, De-Souza EA, Pinto S, Pinca AP, Silva RC, Sato VN, Castilho BA, Mori MA | title = IMPACT is a GCN2 inhibitor that limits lifespan in Caenorhabditis elegans | journal = BMC Biology | volume = 14 | issue = 1 | pages = 87 | date = October 2016 | pmid = 27717342 | doi = 10.1186/s12915-016-0301-2 | url = https://bmcbiol.biomedcentral.com/articles/10.1186/s12915-016-0301-2 }}</ref> | ||
== Translation == | == Translation == | ||
The translation of ATF4 is dependent on [[upstream open reading frame]]s located in the [[5'UTR]].<ref name="Somers_2013">{{cite journal | vauthors = Somers J, Pöyry T, Willis AE | title = A perspective on mammalian upstream open reading frame function | journal = | The translation of ATF4 is dependent on [[upstream open reading frame]]s located in the [[5'UTR]].<ref name="Somers_2013">{{cite journal | vauthors = Somers J, Pöyry T, Willis AE | title = A perspective on mammalian upstream open reading frame function | journal = The International Journal of Biochemistry & Cell Biology | volume = 45 | issue = 8 | pages = 1690–700 | date = August 2013 | pmid = 23624144 | doi = 10.1016/j.biocel.2013.04.020 }}</ref> The location of the second uORF, aptly named uORF2, overlaps with the ''ATF4'' open-reading frame. During normal conditions, the uORF1 is translated, and then translation of uORF2 occurs only after eIF2-TC has been reacquired. Translation of the uORF2 requires that the ribosomes pass by the ''ATF4'' ORF, whose start codon is located within uORF2. This leads to its repression. However, during stress conditions, the [[40S]] ribosome will bypass uORF2 because of a decrease in concentration of eIF2-TC, which means the ribosome does not acquire one in time to translate uORF2. Instead ''ATF4'' is translated.<ref name="Somers_2013"/> | ||
== See also == | == See also == | ||
| Line 20: | Line 20: | ||
== Further reading == | == Further reading == | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Rutkowski DT, Kaufman RJ | title = All roads lead to ATF4 | journal = | * {{cite journal | vauthors = Rutkowski DT, Kaufman RJ | title = All roads lead to ATF4 | journal = Developmental Cell | volume = 4 | issue = 4 | pages = 442–4 | date = April 2003 | pmid = 12689582 | doi = 10.1016/S1534-5807(03)00100-X }} | ||
* {{cite journal | vauthors = Nishizawa M, Nagata S | title = cDNA clones encoding leucine-zipper proteins which interact with G-CSF gene promoter element 1-binding protein | journal = FEBS | * {{cite journal | vauthors = Nishizawa M, Nagata S | title = cDNA clones encoding leucine-zipper proteins which interact with G-CSF gene promoter element 1-binding protein | journal = FEBS Letters | volume = 299 | issue = 1 | pages = 36–8 | date = March 1992 | pmid = 1371974 | doi = 10.1016/0014-5793(92)80094-W }} | ||
* {{cite journal | vauthors = Karpinski BA, Morle GD, Huggenvik J, Uhler MD, Leiden JM | title = Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element | journal = | * {{cite journal | vauthors = Karpinski BA, Morle GD, Huggenvik J, Uhler MD, Leiden JM | title = Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 89 | issue = 11 | pages = 4820–4 | date = June 1992 | pmid = 1534408 | pmc = 49179 | doi = 10.1073/pnas.89.11.4820 }} | ||
* {{cite journal | vauthors = Hai T, Curran T | title = Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity | journal = | * {{cite journal | vauthors = Hai T, Curran T | title = Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 9 | pages = 3720–4 | date = May 1991 | pmid = 1827203 | pmc = 51524 | doi = 10.1073/pnas.88.9.3720 }} | ||
* {{cite journal | vauthors = Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K | title = Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I | journal = | * {{cite journal | vauthors = Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K | title = Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I | journal = Journal of Virology | volume = 65 | issue = 3 | pages = 1420–6 | date = March 1991 | pmid = 1847461 | pmc = 239921 | doi = }} | ||
* {{cite journal | vauthors = Hai TW, Liu F, Coukos WJ, Green MR | title = Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers | journal = Genes | * {{cite journal | vauthors = Hai TW, Liu F, Coukos WJ, Green MR | title = Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers | journal = Genes & Development | volume = 3 | issue = 12B | pages = 2083–90 | date = December 1989 | pmid = 2516827 | doi = 10.1101/gad.3.12b.2083 }} | ||
* {{cite journal | vauthors = Kokame K, Kato H, Miyata T | title = Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes | journal = | * {{cite journal | vauthors = Kokame K, Kato H, Miyata T | title = Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes | journal = The Journal of Biological Chemistry | volume = 271 | issue = 47 | pages = 29659–65 | date = November 1996 | pmid = 8939898 | doi = 10.1074/jbc.271.47.29659 }} | ||
* {{cite journal | vauthors = Reddy TR, Tang H, Li X, Wong-Staal F | title = Functional interaction of the HTLV-1 transactivator Tax with activating transcription factor-4 (ATF4) | journal = Oncogene | volume = 14 | issue = 23 | pages = 2785–92 | | * {{cite journal | vauthors = Reddy TR, Tang H, Li X, Wong-Staal F | title = Functional interaction of the HTLV-1 transactivator Tax with activating transcription factor-4 (ATF4) | journal = Oncogene | volume = 14 | issue = 23 | pages = 2785–92 | date = June 1997 | pmid = 9190894 | doi = 10.1038/sj.onc.1201119 }} | ||
* {{cite journal | vauthors = Liang G, Hai T | title = Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein | journal = | * {{cite journal | vauthors = Liang G, Hai T | title = Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein | journal = The Journal of Biological Chemistry | volume = 272 | issue = 38 | pages = 24088–95 | date = September 1997 | pmid = 9295363 | doi = 10.1074/jbc.272.38.24088 }} | ||
* {{cite journal | vauthors = Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S | title = ZIP | * {{cite journal | vauthors = Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S | title = ZIP kinase, a novel serine/threonine kinase which mediates apoptosis | journal = Molecular and Cellular Biology | volume = 18 | issue = 3 | pages = 1642–51 | date = March 1998 | pmid = 9488481 | pmc = 108879 | doi = 10.1128/mcb.18.3.1642 }} | ||
* {{cite journal | vauthors = Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC | title = Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells | journal = Blood | volume = 94 | issue = 3 | pages = 959–67 | | * {{cite journal | vauthors = Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC | title = Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells | journal = Blood | volume = 94 | issue = 3 | pages = 959–67 | date = August 1999 | pmid = 10419887 | doi = }} | ||
* {{cite journal | vauthors = Podust LM, Krezel AM, Kim Y | title = Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA | journal = | * {{cite journal | vauthors = Podust LM, Krezel AM, Kim Y | title = Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA | journal = The Journal of Biological Chemistry | volume = 276 | issue = 1 | pages = 505–13 | date = January 2001 | pmid = 11018027 | doi = 10.1074/jbc.M005594200 }} | ||
* {{cite journal | vauthors = Murphy P, Kolstø A | title = Expression of the bZIP transcription factor TCF11 and its potential dimerization partners during development | journal = | * {{cite journal | vauthors = Murphy P, Kolstø A | title = Expression of the bZIP transcription factor TCF11 and its potential dimerization partners during development | journal = Mechanisms of Development | volume = 97 | issue = 1-2 | pages = 141–8 | date = October 2000 | pmid = 11025215 | doi = 10.1016/S0925-4773(00)00413-5 }} | ||
* {{cite journal | vauthors = White JH, McIllhinney RA, Wise A, Ciruela F, Chan WY, Emson PC, Billinton A, Marshall FH | title = The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx | journal = | * {{cite journal | vauthors = White JH, McIllhinney RA, Wise A, Ciruela F, Chan WY, Emson PC, Billinton A, Marshall FH | title = The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 25 | pages = 13967–72 | date = December 2000 | pmid = 11087824 | pmc = 17684 | doi = 10.1073/pnas.240452197 }} | ||
* {{cite journal | vauthors = He CH, Gong P, Hu B, Stewart D, Choi ME, Choi AM, Alam J | title = Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation | journal = | * {{cite journal | vauthors = He CH, Gong P, Hu B, Stewart D, Choi ME, Choi AM, Alam J | title = Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 24 | pages = 20858–65 | date = June 2001 | pmid = 11274184 | doi = 10.1074/jbc.M101198200 }} | ||
* {{cite journal | vauthors = Siu F, Bain PJ, LeBlanc-Chaffin R, Chen H, Kilberg MS | title = ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene | journal = | * {{cite journal | vauthors = Siu F, Bain PJ, LeBlanc-Chaffin R, Chen H, Kilberg MS | title = ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene | journal = The Journal of Biological Chemistry | volume = 277 | issue = 27 | pages = 24120–7 | date = July 2002 | pmid = 11960987 | doi = 10.1074/jbc.M201959200 }} | ||
* {{cite journal | vauthors = Bowers AJ, Scully S, Boylan JF | title = SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia | journal = Oncogene | volume = 22 | issue = 18 | pages = 2823–35 | | * {{cite journal | vauthors = Bowers AJ, Scully S, Boylan JF | title = SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia | journal = Oncogene | volume = 22 | issue = 18 | pages = 2823–35 | date = May 2003 | pmid = 12743605 | doi = 10.1038/sj.onc.1206367 }} | ||
* {{cite journal | vauthors = Seo J, Fortuno ES, Suh JM, Stenesen D, Tang W, Parks EJ, Adams CM, Townes T, Graff JM | title = Atf4 | * {{cite journal | vauthors = Seo J, Fortuno ES, Suh JM, Stenesen D, Tang W, Parks EJ, Adams CM, Townes T, Graff JM | title = Atf4 regulates obesity, glucose homeostasis, and energy expenditure | journal = Diabetes | volume = 58 | issue = 11 | pages = 2565–73 | date = November 2009 | pmid = 19690063 | pmc = 2768187 | doi = 10.2337/db09-0335 }} | ||
{{refend}} | {{refend}} | ||
Revision as of 14:18, 3 July 2018
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Activating transcription factor 4 (tax-responsive enhancer element B67), also known as ATF4, is a protein that in humans is encoded by the ATF4 gene.[1][2]
Function
This gene encodes a transcription factor that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB-2). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP-1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein–protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA-binding domain. Two alternative transcripts encoding the same protein have been described. Two pseudogenes are located on the X chromosome at q28 in a region containing a large inverted duplication.[3]
ATF4 transcription factor is also known to play role in osteoblast differentiation along with RUNX2 and osterix.[4] Terminal osteoblast differentiation, represented by matrix mineralization, is significantly inhibited by the inactivation of JNK. JNK inactivation downregulates expression of ATF-4 and, subsequently, matrix mineralization.[5] IMPACT protein regulates ATF4 in C. elegans to promote lifespan.[6]
Translation
The translation of ATF4 is dependent on upstream open reading frames located in the 5'UTR.[7] The location of the second uORF, aptly named uORF2, overlaps with the ATF4 open-reading frame. During normal conditions, the uORF1 is translated, and then translation of uORF2 occurs only after eIF2-TC has been reacquired. Translation of the uORF2 requires that the ribosomes pass by the ATF4 ORF, whose start codon is located within uORF2. This leads to its repression. However, during stress conditions, the 40S ribosome will bypass uORF2 because of a decrease in concentration of eIF2-TC, which means the ribosome does not acquire one in time to translate uORF2. Instead ATF4 is translated.[7]
See also
References
- ↑ Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K (March 1991). "Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I". Journal of Virology. 65 (3): 1420–6. PMC 239921. PMID 1847461.
- ↑ Karpinski BA, Morle GD, Huggenvik J, Uhler MD, Leiden JM (June 1992). "Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element". Proceedings of the National Academy of Sciences of the United States of America. 89 (11): 4820–4. doi:10.1073/pnas.89.11.4820. PMC 49179. PMID 1534408.
- ↑ "Entrez Gene: ATF4 activating transcription factor 4 (tax-responsive enhancer element B67)".
- ↑ Franceschi RT, Ge C, Xiao G, Roca H, Jiang D (2009). "Transcriptional regulation of osteoblasts". Cells Tissues Organs. 189 (1–4): 144–52. doi:10.1159/000151747. PMC 3512205. PMID 18728356.
- ↑ Matsuguchi T, Chiba N, Bandow K, Kakimoto K, Masuda A, Ohnishi T (March 2009). "JNK activity is essential for Atf4 expression and late-stage osteoblast differentiation". Journal of Bone and Mineral Research. 24 (3): 398–410. doi:10.1359/jbmr.081107. PMID 19016586.
- ↑ Ferraz RC, Camara H, De-Souza EA, Pinto S, Pinca AP, Silva RC, Sato VN, Castilho BA, Mori MA (October 2016). "IMPACT is a GCN2 inhibitor that limits lifespan in Caenorhabditis elegans". BMC Biology. 14 (1): 87. doi:10.1186/s12915-016-0301-2. PMID 27717342.
- ↑ 7.0 7.1 Somers J, Pöyry T, Willis AE (August 2013). "A perspective on mammalian upstream open reading frame function". The International Journal of Biochemistry & Cell Biology. 45 (8): 1690–700. doi:10.1016/j.biocel.2013.04.020. PMID 23624144.
Further reading
- Rutkowski DT, Kaufman RJ (April 2003). "All roads lead to ATF4". Developmental Cell. 4 (4): 442–4. doi:10.1016/S1534-5807(03)00100-X. PMID 12689582.
- Nishizawa M, Nagata S (March 1992). "cDNA clones encoding leucine-zipper proteins which interact with G-CSF gene promoter element 1-binding protein". FEBS Letters. 299 (1): 36–8. doi:10.1016/0014-5793(92)80094-W. PMID 1371974.
- Karpinski BA, Morle GD, Huggenvik J, Uhler MD, Leiden JM (June 1992). "Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element". Proceedings of the National Academy of Sciences of the United States of America. 89 (11): 4820–4. doi:10.1073/pnas.89.11.4820. PMC 49179. PMID 1534408.
- Hai T, Curran T (May 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proceedings of the National Academy of Sciences of the United States of America. 88 (9): 3720–4. doi:10.1073/pnas.88.9.3720. PMC 51524. PMID 1827203.
- Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K (March 1991). "Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I". Journal of Virology. 65 (3): 1420–6. PMC 239921. PMID 1847461.
- Hai TW, Liu F, Coukos WJ, Green MR (December 1989). "Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers". Genes & Development. 3 (12B): 2083–90. doi:10.1101/gad.3.12b.2083. PMID 2516827.
- Kokame K, Kato H, Miyata T (November 1996). "Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes". The Journal of Biological Chemistry. 271 (47): 29659–65. doi:10.1074/jbc.271.47.29659. PMID 8939898.
- Reddy TR, Tang H, Li X, Wong-Staal F (June 1997). "Functional interaction of the HTLV-1 transactivator Tax with activating transcription factor-4 (ATF4)". Oncogene. 14 (23): 2785–92. doi:10.1038/sj.onc.1201119. PMID 9190894.
- Liang G, Hai T (September 1997). "Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein". The Journal of Biological Chemistry. 272 (38): 24088–95. doi:10.1074/jbc.272.38.24088. PMID 9295363.
- Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S (March 1998). "ZIP kinase, a novel serine/threonine kinase which mediates apoptosis". Molecular and Cellular Biology. 18 (3): 1642–51. doi:10.1128/mcb.18.3.1642. PMC 108879. PMID 9488481.
- Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC (August 1999). "Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells". Blood. 94 (3): 959–67. PMID 10419887.
- Podust LM, Krezel AM, Kim Y (January 2001). "Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA". The Journal of Biological Chemistry. 276 (1): 505–13. doi:10.1074/jbc.M005594200. PMID 11018027.
- Murphy P, Kolstø A (October 2000). "Expression of the bZIP transcription factor TCF11 and its potential dimerization partners during development". Mechanisms of Development. 97 (1–2): 141–8. doi:10.1016/S0925-4773(00)00413-5. PMID 11025215.
- White JH, McIllhinney RA, Wise A, Ciruela F, Chan WY, Emson PC, Billinton A, Marshall FH (December 2000). "The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx". Proceedings of the National Academy of Sciences of the United States of America. 97 (25): 13967–72. doi:10.1073/pnas.240452197. PMC 17684. PMID 11087824.
- He CH, Gong P, Hu B, Stewart D, Choi ME, Choi AM, Alam J (June 2001). "Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation". The Journal of Biological Chemistry. 276 (24): 20858–65. doi:10.1074/jbc.M101198200. PMID 11274184.
- Siu F, Bain PJ, LeBlanc-Chaffin R, Chen H, Kilberg MS (July 2002). "ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene". The Journal of Biological Chemistry. 277 (27): 24120–7. doi:10.1074/jbc.M201959200. PMID 11960987.
- Bowers AJ, Scully S, Boylan JF (May 2003). "SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia". Oncogene. 22 (18): 2823–35. doi:10.1038/sj.onc.1206367. PMID 12743605.
- Seo J, Fortuno ES, Suh JM, Stenesen D, Tang W, Parks EJ, Adams CM, Townes T, Graff JM (November 2009). "Atf4 regulates obesity, glucose homeostasis, and energy expenditure". Diabetes. 58 (11): 2565–73. doi:10.2337/db09-0335. PMC 2768187. PMID 19690063.
External links
- ATF4+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human ATF4 genome location and ATF4 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
