CREB3

Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Cyclic AMP-responsive element-binding protein 3 is a protein that in humans is encoded by the CREB3 gene.

This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element, an octameric palindrome. The protein interacts with host cell factor C1, which also associates with the herpes simplex virus (HSV) protein VP16 that induces transcription of HSV immediate-early genes. This protein and VP16 both bind to the same site on host cell factor C1. It is thought that the interaction between this protein and host cell factor C1 plays a role in the establishment of latency during HSV infection. An additional transcript variant has been identified, but its biological validity has not been determined.

Interactions

CREB3 has been shown to interact with Host cell factor C1.

See also

• CREB

Further reading

• Freiman RN, Herr W (1998). "Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP". Genes Dev. 11 (23): 3122–7. doi:10.1101/gad.11.23.3122. PMC 316754. PMID 9389645.
• Lu R, Yang P, Padmakumar S, Misra V (1998). "The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF". J. Virol. 72 (8): 6291–7. doi:10.1128/JVI.72.8.6291-6297.1998. PMC 109766. PMID 9658067.
• Lu R, Misra V (2000). "Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency". J. Virol. 74 (2): 934–43. doi:10.1128/JVI.74.2.934-943.2000. PMC 111614. PMID 10623756.
• Mahajan SS, Wilson AC (2000). "Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP". Mol. Cell. Biol. 20 (3): 919–28. doi:10.1128/MCB.20.3.919-928.2000. PMC 85209. PMID 10629049.
• Jin DY, Wang HL, Zhou Y, et al. (2000). "Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation". EMBO J. 19 (4): 729–40. doi:10.1093/emboj/19.4.729. PMC 305611. PMID 10675342.
• Luciano RL, Wilson AC (2000). "N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10757–62. Bibcode:2000PNAS...9710757L. doi:10.1073/pnas.190062797. PMC 27096. PMID 10984507.
• Raggo C, Rapin N, Stirling J, et al. (2002). "Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis". Mol. Cell. Biol. 22 (16): 5639–49. doi:10.1128/MCB.22.16.5639-5649.2002. PMC 133973. PMID 12138176.
• Mahajan SS, Little MM, Vazquez R, Wilson AC (2003). "Interaction of HCF-1 with a cellular nuclear export factor". J. Biol. Chem. 277 (46): 44292–9. doi:10.1074/jbc.M205440200. PMC 4291127. PMID 12235138.
• Luciano RL, Wilson AC (2002). "An activation domain in the C-terminal subunit of HCF-1 is important for transactivation by VP16 and LZIP". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13403–8. Bibcode:2002PNAS...9913403L. doi:10.1073/pnas.202200399. PMC 129685. PMID 12271126.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ko J, Jang SW, Kim YS, et al. (2004). "Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines". FASEB J. 18 (7): 890–2. doi:10.1096/fj.03-0867fje. PMID 15001559. S2CID 24742296.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Misra V, Rapin N, Akhova O, et al. (2005). "Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman". J. Biol. Chem. 280 (15): 15257–66. doi:10.1074/jbc.M500728200. PMID 15705566.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Liang G, Audas TE, Li Y, et al. (2007). "Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element". Mol. Cell. Biol. 26 (21): 7999–8010. doi:10.1128/MCB.01046-06. PMC 1636730. PMID 16940180.
• Blot G, Lopez-Vergès S, Treand C, et al. (2007). "Luman, a new partner of HIV-1 TMgp41, interferes with Tat-mediated transcription of the HIV-1 LTR". J. Mol. Biol. 364 (5): 1034–47. doi:10.1016/j.jmb.2006.09.080. PMID 17054986.
• Jang SW, Kim YS, Lee YH, Ko J (2007). "Role of human LZIP in differential activation of the NF-kappaB pathway that is induced by CCR1-dependent chemokines". J. Cell. Physiol. 211 (3): 630–7. doi:10.1002/jcp.20968. PMID 17192849. S2CID 40274182.
• Jang SW, Kim YS, Kim YR, et al. (2007). "Regulation of human LZIP expression by NF-kappaB and its involvement in monocyte cell migration induced by Lkn-1". J. Biol. Chem. 282 (15): 11092–100. doi:10.1074/jbc.M607962200. PMID 17296613.

External links

• CREB3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Template:UCSC gene info

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

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