Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction
Open accessAbstract
The pivotal role that protein-tyrosine kinases (PTKs) play in the growth regulation of eukaryotic cells is manifest in the frequent appearance of members of the PTK family as growth factor receptors or as the transforming agents of acutely transforming retroviruses. A feature common to all members of the PTK family is a highly conserved catalytic domain which is characteristic of the group as a whole and whose activity appears to be tightly regulated within the cell by other domains of the PTK. Degenerate oligonucleotide probes corresponding to two invariant amino acid sequence motifs within the catalytic domains of all PTK family members were synthesized and employed in the polymerase chain reaction (PCR) to amplify cDNA sequences between them. An M13 PCR library was produced in this way from cDNA prepared against mRNA from the murine hemopoietic cell line FDC-P1. The PCR library was then screened by DNA sequencing for PTK-related sequences. Two sequences were identified that, on the basis of sequence comparison with known PTKs, may encode representatives of a new class of PTK.
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The human genome encodes four JAKs: JAK1, JAK2, JAK3, and TYK2.
“The human genome encodes four JAKs—JAK1, JAK2, JAK3, and tyrosine kinase 2 (TYK2)—that associate selectively (Fig. 1) with different receptors (Wilks, 1989; Firmbach-Kraft et al., 1990; Wilks et al., 1991; Harpur et al., 1992).”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as Wilks, 1989
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Dumont, D. J., Gradwohl, G., Fong, G. H., Puri, M. C., Gertsenstein, M., Auerbach, A., & Breitman, M. L. (1994) · Genes & Development · doi:10.1101/gad.8.16.1897 · Cited by 985 · see citing works
Small, D., Levenstein, M., Kim, E., Carow, C., Amin, S., Rockwell, P., Witte, L., Burrow, C., Ratajczak, M. Z., & Gewirtz, A. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.459 · Cited by 429 · see citing works
Bharadwaj, U., Kasembeli, M. M., Robinson, P., & Tweardy, D. J. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018440 · Cited by 314 · see citing works
“1) with different receptors (Wilks, 1989; Firmbach-Kraft et al., 1990; Wilks et al., 1991; Harpur et al., 1992).”
BackgroundKershaw, N. J., Murphy, J. M., Liau, N. P. D., Varghese, L. N., Laktyushin, A., Whitlock, E. L., Lucet, I. S., Nicola, N. A., & Babon, J. J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2519 · Cited by 301 · see citing works
STAT1 from the cell membrane to the DNA
Lillemeier, B. F., Köster, M., & Kerr, I. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2508 · Cited by 88 · see citing works
Ng, I. H. W., Ng, D. C. H., Jans, D. A., & Bogoyevitch, M. A. (2012) · Biochemical Journal · doi:10.1042/bj20120941 · Cited by 63 · see citing works
“31 Wilks, A. F. (1989) Two putative protein-tyrosine kinases identified by application of the”
BackgroundZhang, H.-Y., Jin, X.-B., & Lue, T. F. (2011) · Asian Journal of Andrology · doi:10.1038/aja.2010.162 · Cited by 39 · see citing works
A search for tyrosine kinase receptors expressed in the rat embryonic pancreas
LeBras, S., Czernichow, P., & Scharfmann, R. (1998) · Diabetologia · doi:10.1007/s001250051094 · Cited by 35 · see citing works
- Authors
- Wilks, A. F.
- Affiliations
- The Royal Melbourne Hospital (AU)
- Corresponding author
- Wilks, A F
- ORCID
- Wilks, A F
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1989-03
- Volume
- 86
- Issue
- 5
- Pages
- 1603-1607
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC286746
- OpenAlex
- W2016188929
- Cited by
- 424
- References
- 0
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 10 · 2023: 9 · 2022: 11 · 2021: 5 · 2020: 5 · 2019: 3 · 2018: 5 · 2017: 6 · 2016: 6 · 2015: 7 · 2014: 7 · 2013: 10 · 2012: 14
- FWCI
- 6.69
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
- Keywords
- tyrosine kinase, catalytic domain, cDNA cloning, growth factor receptors, growth regulation
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Cloning, Molecular, Gene Amplification, Genes, Multigene Family, Molecular Sequence Data, Poly A, Protein-Tyrosine Kinases, RNA, RNA, Messenger, Mice
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