The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Serine-arginine protein kinases: a small protein kinase family with a large cellular presence
Abstract
Serine-arginine protein kinases (SPRKs) constitute a relatively novel subfamily of serine-threonine kinases that specifically phosphorylate serine residues residing in serine-arginine/arginine-serine dipeptide motifs. Fifteen years of research subsequent to the purification and cloning of human SRPK1 as a SR splicing factor-phosphorylating protein have lead to the accumulation of information on the function and regulation of the different members of this family, as well as on the genomic organization of SRPK genes in several organisms. Originally considered to be devoted to constitutive and alternative mRNA splicing, SRPKs are now known to expand their influence to additional steps of mRNA maturation, as well as to other cellular activities, such as chromatin reorganization in somatic and sperm cells, cell cycle and p53 regulation, and metabolic signalling. Similarly, SRPKs were considered to be constitutively active kinases, although several modes of regulation of their function have been demonstrated, implying an elaborate cellular control of their activity. Finally, SRPK gene sequence information from bioinformatics data reveals that SRPK gene homologs exist either in single or multiple copies in every single eukaryotic organism tested, emphasizing the importance of SRPK protein function for cellular life.
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Cites
Metabolic control through the PGC-1 family of transcription coactivators
Lin, J., Handschin, C., & Spiegelman, B. M. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.004 · Cited by 2,130
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487
Signaling to Chromatin through Histone Modifications
Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989
Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.007 · Cited by 594
Akt/PKB regulates hepatic metabolism by directly inhibiting PGC-1α transcription coactivator
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“SRPK1 catalyzes phosphorylation of mRNA-processing factors including ASF/SF2 (Giannakouros et al., 2011).”
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Metadata
- Authors
- Giannakouros, T., Nikolakaki, E., Mylonis, I., & Georgatsou, E.
- Venue
- FEBS Journal
- Publisher
- Wiley
- Published
- 2011-01-12
- Volume
- 278
- Issue
- 4
- Pages
- 570-586
- ISSN
- 1742-464X (ISSN-L)
- OpenAlex
- W1591518654
- Cited by
- 188
- References
- 5
- FWCI
- 2.60
- Type
- journal article
- Language
- en
- Open access
- closed
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- Giannakouros, T., Nikolakaki, E., Mylonis, I., & Georgatsou, E. (2011). Serine-arginine protein kinases: a small protein kinase family with a large cellular presence. FEBS Journal. https://doi.org/10.1111/j.1742-4658.2010.07987.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
