Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs - PubMed (original) (raw)
Comparative Study
. 1992 Feb 14;182(3):1416-22.
doi: 10.1016/0006-291x(92)91891-s.
Affiliations
- PMID: 1540184
- DOI: 10.1016/0006-291x(92)91891-s
Comparative Study
Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs
H Owaki et al. Biochem Biophys Res Commun. 1992.
Abstract
Extracellular signal-regulated kinases 1 and 2 are growth factor-sensitive serine/threonine kinases. cDNAs for both human kinases were isolated and sequenced. The nucleic acid and deduced protein sequences of human extracellular signal-regulated kinase 1 were 88% and 96% identical, respectively, to the homologous rat sequences. The nucleic acid and deduced protein sequences of human extracellular signal-regulated kinase 2 were 90% and 98% identical, respectively, to the corresponding rat sequences. A human extracellular signal-regulated kinase 2 specific probe was used to demonstrate that the mRNA for this kinase was present in T cells and did not change with activation. The deduced protein sequences of both human kinases were greater than 95% identical to two Xenopus kinase sequences, indicating that these enzymes are highly conserved across species.
Similar articles
- ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF.
Boulton TG, Nye SH, Robbins DJ, Ip NY, Radziejewska E, Morgenbesser SD, DePinho RA, Panayotatos N, Cobb MH, Yancopoulos GD. Boulton TG, et al. Cell. 1991 May 17;65(4):663-75. doi: 10.1016/0092-8674(91)90098-j. Cell. 1991. PMID: 2032290 - Existence of two isoforms of extracellular signal-regulated kinase in fish.
Hashimoto H, Yokoyama Y, Matsuo Y, Toyohara H, Kohno M, Sakaguchi M. Hashimoto H, et al. J Biochem. 1998 Jun;123(6):1031-5. doi: 10.1093/oxfordjournals.jbchem.a022039. J Biochem. 1998. PMID: 9603989 - The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
Hanks SK, Quinn AM, Hunter T. Hanks SK, et al. Science. 1988 Jul 1;241(4861):42-52. doi: 10.1126/science.3291115. Science. 1988. PMID: 3291115 Review.
Cited by
- ERBB2 Targeting Reveals a Significant Suppression of Tumorigenesis in Murine Endometrial Cancer with Pten Mutation.
Dunston K, Hunter MI, Johannesen E, Jung JS, Kim TH, Yoo JY, Jeong JW. Dunston K, et al. Reprod Sci. 2024 Aug;31(8):2458-2467. doi: 10.1007/s43032-024-01546-3. Epub 2024 Apr 18. Reprod Sci. 2024. PMID: 38637476 - Unique evolution of foraminiferal calcification to survive global changes.
Ujiié Y, Ishitani Y, Nagai Y, Takaki Y, Toyofuku T, Ishii S. Ujiié Y, et al. Sci Adv. 2023 Jun 23;9(25):eadd3584. doi: 10.1126/sciadv.add3584. Epub 2023 Jun 21. Sci Adv. 2023. PMID: 37343099 Free PMC article. - LINC00511 promotes cervical cancer progression by regulating the miR-497-5p/MAPK1 axis.
Lu M, Gao Q, Wang Y, Ren J, Zhang T. Lu M, et al. Apoptosis. 2022 Dec;27(11-12):800-811. doi: 10.1007/s10495-022-01768-3. Epub 2022 Sep 14. Apoptosis. 2022. PMID: 36103025 Free PMC article. - MAPK1 up-regulates the expression of MALAT1 to promote the proliferation of cardiomyocytes through PI3K/AKT signaling pathway.
Zhao J, Li L, Peng L. Zhao J, et al. Int J Clin Exp Pathol. 2015 Dec 1;8(12):15947-53. eCollection 2015. Int J Clin Exp Pathol. 2015. PMID: 26884868 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous