Ligand interaction scan (LIScan) in the study of ERK8 - PubMed (original) (raw)
. 2010 Aug 13;399(1):37-41.
doi: 10.1016/j.bbrc.2010.07.029. Epub 2010 Jul 16.
Affiliations
- PMID: 20638370
- DOI: 10.1016/j.bbrc.2010.07.029
Ligand interaction scan (LIScan) in the study of ERK8
Oran Erster et al. Biochem Biophys Res Commun. 2010.
Abstract
ERK8 is the most recent addition for the MAPK family, and its mechanism of activation and function are not yet known, mainly due to the lack of any known physiological stimulator. In this report, we describe the preparation of reagents for the use of a novel method, the ligand interaction scan (LIScan), to study the function of this protein kinase. We generated a set of mutants of ERK8, and identified inhibited as well as stimulated forms. By specifically inhibiting or stimulating the mutants of ERK8, we show that the ERK8-induced inhibition of proliferation is altered. Moreover, we used the developed mutants to show for the first time that ERK8 translocates to the nucleus upon activation. The use of methods such as the ligand interaction scan may thus promote the analyses of the functions of uncharacterized proteins such as ERK8, and possibly help in controlling the activity of target proteins in various experimental systems and applications.
2010 Elsevier Inc. All rights reserved.
Similar articles
- Extracellular signal-regulated kinase 8 (ERK8) controls estrogen-related receptor α (ERRα) cellular localization and inhibits its transcriptional activity.
Rossi M, Colecchia D, Iavarone C, Strambi A, Piccioni F, Verrotti di Pianella A, Chiariello M. Rossi M, et al. J Biol Chem. 2011 Mar 11;286(10):8507-8522. doi: 10.1074/jbc.M110.179523. Epub 2010 Dec 28. J Biol Chem. 2011. PMID: 21190936 Free PMC article. - Characterization of the reversible phosphorylation and activation of ERK8.
Klevernic IV, Stafford MJ, Morrice N, Peggie M, Morton S, Cohen P. Klevernic IV, et al. Biochem J. 2006 Feb 15;394(Pt 1):365-73. doi: 10.1042/BJ20051288. Biochem J. 2006. PMID: 16336213 Free PMC article. - A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA.
Groehler AL, Lannigan DA. Groehler AL, et al. J Cell Biol. 2010 Aug 23;190(4):575-86. doi: 10.1083/jcb.201002124. J Cell Biol. 2010. PMID: 20733054 Free PMC article. - Purification and characterization of a highly specific polyclonal antibody against human extracellular signal-regulated kinase 8 and its detection in lung cancer.
Cai NL, Lau ATY, Yu FY, Wu DD, Dai LJ, Mo HY, Lin CM, Xu YM. Cai NL, et al. PLoS One. 2017 Sep 13;12(9):e0184755. doi: 10.1371/journal.pone.0184755. eCollection 2017. PLoS One. 2017. PMID: 28902877 Free PMC article. - Cellular and physiological roles of the conserved atypical MAP kinase ERK7.
Deniz O, Hasygar K, Hietakangas V. Deniz O, et al. FEBS Lett. 2023 Mar;597(5):601-607. doi: 10.1002/1873-3468.14521. Epub 2022 Oct 28. FEBS Lett. 2023. PMID: 36266944 Review.
Cited by
- ERK7 is a negative regulator of protein secretion in response to amino-acid starvation by modulating Sec16 membrane association.
Zacharogianni M, Kondylis V, Tang Y, Farhan H, Xanthakis D, Fuchs F, Boutros M, Rabouille C. Zacharogianni M, et al. EMBO J. 2011 Aug 16;30(18):3684-700. doi: 10.1038/emboj.2011.253. EMBO J. 2011. PMID: 21847093 Free PMC article. - Inactivation of Sirt6 ameliorates muscular dystrophy in mdx mice by releasing suppression of utrophin expression.
Georgieva AM, Guo X, Bartkuhn M, Günther S, Künne C, Smolka C, Atzberger A, Gärtner U, Mamchaoui K, Bober E, Zhou Y, Yuan X, Braun T. Georgieva AM, et al. Nat Commun. 2022 Jul 20;13(1):4184. doi: 10.1038/s41467-022-31798-z. Nat Commun. 2022. PMID: 35859073 Free PMC article. - High-throughput analysis of an RNAi library identifies novel kinase targets in Trypanosoma brucei.
Mackey ZB, Koupparis K, Nishino M, McKerrow JH. Mackey ZB, et al. Chem Biol Drug Des. 2011 Sep;78(3):454-63. doi: 10.1111/j.1747-0285.2011.01156.x. Epub 2011 Jul 14. Chem Biol Drug Des. 2011. PMID: 21668652 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases