ArticleThe Journal of biological chemistry2015
Regulation of Catalytic and Non-catalytic Functions of the Drosophila Ste20 Kinase Slik by Activation Segment Phosphorylation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Identification of a Ste20-like kinase-dependent signaling network orchestrating cytoskeletal and synaptic development of cortical neurons.Cell communication and signaling : CCS · 2026Article
- Review
- Slik maintains tissue homeostasis by preventing JNK-mediated apoptosis.Cell division · 2023Article
- Ste20-like kinase activity promotes meiotic resumption and spindle microtubule stability in mouse oocytes.Cell proliferation · 2023Article
- STRIPAK regulates Slik localization to control mitotic morphogenesis and epithelial integrity.The Journal of cell biology · 2020Article
- Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms.Nature cell biology · 2020Article
- Insights into evolutionary interaction patterns of the 'Phosphorylation Activation Segment' in kinase.Bioinformation · 2019Article
- Moesin is involved in polarity maintenance and cortical remodeling during asymmetric cell division.Molecular biology of the cell · 2018Article
- Regulation of Ste20-like kinase, SLK, activity: Dimerization and activation segment phosphorylation.PloS one · 2017Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinases carry out important functions in cells both by phosphorylating substrates and by means of regulated non-catalytic activities. Such non-catalytic functions have been ascribed to many kinases, including some members of the Ste20 family. The Drosophila Ste20 kinase Slik phosphorylates and activates Moesin in developing epithelial tissues to promote epithelial tissue integrity. It also functions non-catalytically to promote epithelial cell proliferation and tissue growth. We carried out a structure-function analysis to determine how these two distinct activities of Slik are controlled. We find that the conserved C-terminal coiled-coil domain of Slik, which is necessary and sufficient for apical localization of the kinase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-promoting function of Slik. Slik is auto- and trans-phosphorylated in vivo. Phosphorylation of at least two of three conserved sites in the activation segment is required for both efficient catalytic activity and non-catalytic signaling. Slik function is thus dependent upon proper localization of the kinase via the C-terminal coiled-coil domain and activation via activation segment phosphorylation, which enhances both phosphorylation of substrates like Moesin and engagement of effectors of its non-catalytic growth-promoting activity.
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