ArticleJournal of cell science2010
Sip1, the Drosophila orthologue of EBP50/NHERF1, functions with the sterile 20 family kinase Slik to regulate Moesin activity.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- ERM-1 Phosphorylation and NRFL-1 Redundantly Control Lumen Formation in theFrontiers in cell and developmental biology · 2022Article
- Targeted renal knockdown of NaAmerican journal of physiology. Renal physiology · 2019Article
- Role of the PDZ-scaffold protein NHERF1/EBP50 in cancer biology: from signaling regulation to clinical relevance.Oncogene · 2017Review
- The ecdysone receptor signalling regulates microvilli formation in follicular epithelial cells.Cellular and molecular life sciences : CMLS · 2016Article
- Dynamics of ezrin and EBP50 in regulating microvilli on the apical aspect of epithelial cells.Biochemical Society transactions · 2014Article
- Slik and the receptor tyrosine kinase Breathless mediate localized activation of Moesin in terminal tracheal cells.PloS one · 2014Article
- Interactome analysis reveals ezrin can adopt multiple conformational states.The Journal of biological chemistry · 2013Article
- Focal defects in single-celled tubes mutant for Cerebral cavernous malformation 3, GCKIII, or NSF2.Developmental cell · 2013Article
- Article
- Ezrin-mediated apical integrity is required for intestinal homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
Organization of the plasma membrane in polarized epithelial cells is accomplished by the specific localization of transmembrane or membrane-associated proteins, which are often linked to cytoplasmic protein complexes, including the actin cytoskeleton. In this study, we identified Sip1 as a Drosophila orthologue of the ezrin-radixin-moesin (ERM) binding protein 50 (EBP50; also known as the Na(+)/H(+) exchanger regulatory factor NHERF1). In mammals, EBP50/NHERF1 is a scaffold protein required for the regulation of several transmembrane receptors and downstream signal transduction activity. In Drosophila, loss of Sip1 leads to a reduction in Slik kinase protein abundance, loss of Moesin phosphorylation and changes in epithelial structure, including mislocalization of E-cadherin and F-actin. Consistent with these findings, Moesin and Sip1 act synergistically in genetic-interaction experiments, and Sip1 protein abundance is dependent on Moesin. Co-immunoprecipitation experiments indicate that Sip1 forms a complex with both Moesin and Slik. Taken together, these data suggest that Sip1 promotes Slik-dependent phosphorylation of Moesin, and suggests a mechanism for the regulation of Moesin activity within the cell to maintain epithelial integrity.
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