ATF3

ATF3
Identificadores
Nomes alternativos	ATF3
IDs externos	OMIM: 603148 HomoloGene: 1265 GeneCards: ATF3
Ontologia genética
Função molecular	• GO:0000975 transcription cis-regulatory region binding; • protein homodimerization activity; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • RNA polymerase II transcription regulatory region sequence-specific DNA binding; • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific; • protein heterodimerization activity; • identical protein binding; • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific; • DNA binding; • GO:0001106 transcription corepressor activity; • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific;
Componente celular	• nucléolo; • cariolinfa; • CHOP-ATF3 complex; • núcleo celular;
Processo biológico	• GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II; • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; • positive regulation of cell population proliferation; • skeletal muscle cell differentiation; • regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; • gliconeogênese; • cellular response to amino acid starvation; • GO:0045996 negative regulation of transcription, DNA-templated; • GO:0009373 regulation of transcription, DNA-templated; • positive regulation of TRAIL-activated apoptotic signaling pathway; • transcription, DNA-templated; • GO:1901313 positive regulation of gene expression; • PERK-mediated unfolded protein response; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • negative regulation of ERK1 and ERK2 cascade; • GO:1901227 negative regulation of transcription by RNA polymerase II; • Resposta a proteínas mal enoveladas; • transcription by RNA polymerase II; • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	Mais dados de referência de expressão
Ortólogos
	467
	n/a
	ENSG00000162772
	n/a
	P18847
	n/a
NM_001030287; NM_001040619; NM_001206484; NM_001206485; NM_001206486;
	NM_001206488; NM_001674; NM_004024
	n/a
NP_001025458; NP_001035709; NP_001193413; NP_001193415; NP_001193417;
	NP_001665
	n/a
	Wikidata
Ver/Editar Humano

A Fator de transcrição dependente de AMP cíclico ATF-3 é uma proteína que em humanos é codificada pelo gene ATF3.^[2]

Função

O fator de transcrição de ativação 3 é um membro da família de fatores de transcrição da proteína fator de transcrição de ativação dos mamíferos/proteína de ligação ao elemento cAMP (CREB) de resposta ao cAMP. Múltiplas variantes de transcrição que codificam duas isoformas diferentes foram encontradas para esse gene. A isoforma mais longa reprime em vez de ativar a transcrição de promotores com elementos de ligação ao ATF. A isoforma mais curta (deltaZip2) não possui o motivo de dimerização da proteína do zíper de leucina e não se liga ao DNA e estimula a transcrição, presume-se, sequestrando co-fatores inibidores para longe do promotor. É possível que o processamento alternativo do gene ATF3 possa ser fisiologicamente importante na regulação dos genes alvo.^[3]

Significado clínico

O ATF-3 é induzido por estresse fisiológico em vários tecidos. É também um marcador de regeneração após lesão de neurônios do gânglio da raiz dorsal, pois os neurônios regeneradores lesionados ativam esse fator de transcrição. Estudos de validação funcional mostraram que o ATF3 pode promover a regeneração de neurônios periféricos, mas não é capaz de promover a regeneração de neurônios do sistema nervoso central.^[4]^[5]

Interações

Demonstrou-se que o ATF3 interage com:

Leitura adicional

Hai TW, Liu F, Coukos WJ, Green MR (dezembro de 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. PMID 2516827. doi:10.1101/gad.3.12b.2083
Kaszubska W, Hooft van Huijsduijnen R, Ghersa P, DeRaemy-Schenk AM, Chen BP, Hai T, DeLamarter JF, Whelan J (novembro de 1993). «Cyclic AMP-independent ATF family members interact with NF-kappa B and function in the activation of the E-selectin promoter in response to cytokines». Molecular and Cellular Biology. 13 (11): 7180–90. PMC 364779. PMID 7692236. doi:10.1128/MCB.13.11.7180
Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (janeiro de 1994). «Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression». Molecular Endocrinology. 8 (1): 59–68. PMID 8152431. doi:10.1210/mend.8.1.8152431
Liang G, Wolfgang CD, Chen BP, Chen TH, Hai T (janeiro de 1996). «ATF3 gene. Genomic organization, promoter, and regulation». The Journal of Biological Chemistry. 271 (3): 1695–701. PMID 8576171. doi:10.1074/jbc.271.3.1695
Chen BP, Wolfgang CD, Hai T (março de 1996). «Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10». Molecular and Cellular Biology. 16 (3): 1157–68. PMC 231098. PMID 8622660. doi:10.1128/MCB.16.3.1157
Hagmeyer BM, Duyndam MC, Angel P, de Groot RP, Verlaan M, Elfferich P, van der Eb A, Zantema A (março de 1996). «Altered AP-1/ATF complexes in adenovirus-E1-transformed cells due to EIA-dependent induction of ATF3». Oncogene. 12 (5): 1025–32. PMID 8649793
Allan AL, Albanese C, Pestell RG, LaMarre J (julho de 2001). «Activating transcription factor 3 induces DNA synthesis and expression of cyclin D1 in hepatocytes». The Journal of Biological Chemistry. 276 (29): 27272–80. PMID 11375399. doi:10.1074/jbc.M103196200
Zhang C, Kawauchi J, Adachi MT, Hashimoto Y, Oshiro S, Aso T, Kitajima S (dezembro de 2001). «Activation of JNK and transcriptional repressor ATF3/LRF1 through the IRE1/TRAF2 pathway is implicated in human vascular endothelial cell death by homocysteine». Biochemical and Biophysical Research Communications. 289 (3): 718–24. PMID 11726207. doi:10.1006/bbrc.2001.6044
Yan C, Wang H, Boyd DD (março de 2002). «ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter». The Journal of Biological Chemistry. 277 (13): 10804–12. PMID 11792711. doi:10.1074/jbc.M112069200
Shaheduzzaman S, Krishnan V, Petrovic A, Bittner M, Meltzer P, Trent J, Venkatesan S, Zeichner S (2002). «Effects of HIV-1 Nef on cellular gene expression profiles». Journal of Biomedical Science. 9 (1): 82–96. PMID 11810028. doi:10.1007/BF02256581
Hashimoto Y, Zhang C, Kawauchi J, Imoto I, Adachi MT, Inazawa J, Amagasa T, Hai T, Kitajima S (junho de 2002). «An alternatively spliced isoform of transcriptional repressor ATF3 and its induction by stress stimuli». Nucleic Acids Research. 30 (11): 2398–406. PMC 117192. PMID 12034827. doi:10.1093/nar/30.11.2398
Kawauchi J, Zhang C, Nobori K, Hashimoto Y, Adachi MT, Noda A, Sunamori M, Kitajima S (outubro de 2002). «Transcriptional repressor activating transcription factor 3 protects human umbilical vein endothelial cells from tumor necrosis factor-alpha-induced apoptosis through down-regulation of p53 transcription». The Journal of Biological Chemistry. 277 (41): 39025–34. PMID 12161427. doi:10.1074/jbc.M202974200
Zhang C, Gao C, Kawauchi J, Hashimoto Y, Tsuchida N, Kitajima S (outubro de 2002). «Transcriptional activation of the human stress-inducible transcriptional repressor ATF3 gene promoter by p53». Biochemical and Biophysical Research Communications. 297 (5): 1302–10. PMID 12372430. doi:10.1016/S0006-291X(02)02382-3
Fan F, Jin S, Amundson SA, Tong T, Fan W, Zhao H, Zhu X, Mazzacurati L, Li X, Petrik KL, Fornace AJ, Rajasekaran B, Zhan Q (outubro de 2002). «ATF3 induction following DNA damage is regulated by distinct signaling pathways and over-expression of ATF3 protein suppresses cells growth». Oncogene. 21 (49): 7488–96. PMID 12386811. doi:10.1038/sj.onc.1205896
Nobori K, Ito H, Tamamori-Adachi M, Adachi S, Ono Y, Kawauchi J, Kitajima S, Marumo F, Isobe M (outubro de 2002). «ATF3 inhibits doxorubicin-induced apoptosis in cardiac myocytes: a novel cardioprotective role of ATF3». Journal of Molecular and Cellular Cardiology. 34 (10): 1387–97. PMID 12392999. doi:10.1006/jmcc.2002.2091
Kang Y, Chen CR, Massagué J (abril de 2003). «A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells». Molecular Cell. 11 (4): 915–26. PMID 12718878. doi:10.1016/S1097-2765(03)00109-6
Newman JR, Keating AE (junho de 2003). «Comprehensive identification of human bZIP interactions with coiled-coil arrays». Science. 300 (5628): 2097–101. PMID 12805554. doi:10.1126/science.1084648
Kool J, Hamdi M, Cornelissen-Steijger P, van der Eb AJ, Terleth C, van Dam H (julho de 2003). «Induction of ATF3 by ionizing radiation is mediated via a signaling pathway that includes ATM, Nibrin1, stress-induced MAPkinases and ATF-2». Oncogene. 22 (27): 4235–42. PMID 12833146. doi:10.1038/sj.onc.1206611

Referências

↑ «Human PubMed Reference:»
↑ Chen BP, Liang G, Whelan J, Hai T (junho de 1994). «ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms». The Journal of Biological Chemistry. 269 (22): 15819–26. PMID 7515060
↑ «Entrez Gene: ATF3 activating transcription factor 3»
↑ Chen BP, Wolfgang CD, Hai T (março de 1996). «Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10». Molecular and Cellular Biology. 16 (3): 1157–68. PMC 231098. PMID 8622660. doi:10.1128/MCB.16.3.1157
↑ Lindå H, Sköld MK, Ochsmann T (2011). «Activating transcription factor 3, a useful marker for regenerative response after nerve root injury». Frontiers in Neurology. 2. 30 páginas. PMC 3099310. PMID 21629765. doi:10.3389/fneur.2011.00030
↑ Pearson AG, Gray CW, Pearson JF, Greenwood JM, During MJ, Dragunow M (dezembro de 2003). «ATF3 enhances c-Jun-mediated neurite sprouting». Brain Research. Molecular Brain Research. 120 (1): 38–45. PMID 14667575. doi:10.1016/j.molbrainres.2003.09.014
↑ ^a ^b Chen BP, Wolfgang CD, Hai T (março de 1996). «Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10». Molecular and Cellular Biology. 16 (3): 1157–68. PMC 231098. PMID 8622660. doi:10.1128/MCB.16.3.1157
↑ Hai T, Curran T (maio de 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. PMC 51524. PMID 1827203. doi:10.1073/pnas.88.9.3720
↑ Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (janeiro de 1994). «Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression». Molecular Endocrinology. 8 (1): 59–68. PMID 8152431. doi:10.1210/mend.8.1.8152431
↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (setembro de 2005). «A human protein-protein interaction network: a resource for annotating the proteome». Cell. 122 (6): 957–68. PMID 16169070. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0
↑ Yan C, Wang H, Boyd DD (março de 2002). «ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter». The Journal of Biological Chemistry. 277 (13): 10804–12. PMID 11792711. doi:10.1074/jbc.M112069200
↑ Kang Y, Chen CR, Massagué J (abril de 2003). «A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells». Molecular Cell. 11 (4): 915–26. PMID 12718878. doi:10.1016/s1097-2765(03)00109-6

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[1] «Human PubMed Reference:»

[pmid7515060-2] Chen BP, Liang G, Whelan J, Hai T (junho de 1994). «ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms». The Journal of Biological Chemistry. 269 (22): 15819–26. PMID 7515060

[entrez-3] «Entrez Gene: ATF3 activating transcription factor 3»

[4] Chen BP, Wolfgang CD, Hai T (março de 1996). «Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10». Molecular and Cellular Biology. 16 (3): 1157–68. PMC 231098. PMID 8622660. doi:10.1128/MCB.16.3.1157

[pmid21629765-5] Lindå H, Sköld MK, Ochsmann T (2011). «Activating transcription factor 3, a useful marker for regenerative response after nerve root injury». Frontiers in Neurology. 2. 30 páginas. PMC 3099310. PMID 21629765. doi:10.3389/fneur.2011.00030

[pmid14667575-6] Pearson AG, Gray CW, Pearson JF, Greenwood JM, During MJ, Dragunow M (dezembro de 2003). «ATF3 enhances c-Jun-mediated neurite sprouting». Brain Research. Molecular Brain Research. 120 (1): 38–45. PMID 14667575. doi:10.1016/j.molbrainres.2003.09.014

[pmid8622660-7] Chen BP, Wolfgang CD, Hai T (março de 1996). «Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10». Molecular and Cellular Biology. 16 (3): 1157–68. PMC 231098. PMID 8622660. doi:10.1128/MCB.16.3.1157

[pmid1827203-8] Hai T, Curran T (maio de 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. PMC 51524. PMID 1827203. doi:10.1073/pnas.88.9.3720

[pmid8152431-9] Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (janeiro de 1994). «Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression». Molecular Endocrinology. 8 (1): 59–68. PMID 8152431. doi:10.1210/mend.8.1.8152431

[pmid16169070-10] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (setembro de 2005). «A human protein-protein interaction network: a resource for annotating the proteome». Cell. 122 (6): 957–68. PMID 16169070. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0

[pmid11792711-11] Yan C, Wang H, Boyd DD (março de 2002). «ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter». The Journal of Biological Chemistry. 277 (13): 10804–12. PMID 11792711. doi:10.1074/jbc.M112069200

[pmid12718878-12] Kang Y, Chen CR, Massagué J (abril de 2003). «A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells». Molecular Cell. 11 (4): 915–26. PMID 12718878. doi:10.1016/s1097-2765(03)00109-6

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