ArticleThe Journal of biological chemistry2009
Intramolecular interactions between the SRC homology 3 and guanylate kinase domains of discs large regulate its function in asymmetric cell division.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- From the Making of a Neural Lineage to the Making of a Tumor: Lessons from the "Simple" Drosophila Brain.Advances in experimental medicine and biology · 2025Review
- Evidence for a nuclear role forMolecular biology of the cell · 2021Article
- Genetic variants of SDCCAG8 and MAGI2 in mitosis-related pathway genes are independent predictors of cutaneous melanoma-specific survival.Cancer science · 2021Article
- Distinct activities of Scrib module proteins organize epithelial polarity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-κB signaling upon T cell activation.Cell communication and signaling : CCS · 2014Article
- Dishevelled binds the Discs large 'Hook' domain to activate GukHolder-dependent spindle positioning in Drosophila.PloS one · 2014Article
- Protein kinase Cα promotes cell migration through a PDZ-dependent interaction with its novel substrate discs large homolog 1 (DLG1).The Journal of biological chemistry · 2011Article
- Characterization of the Src/Abl hybrid kinase SmTK6 of Schistosoma mansoni.The Journal of biological chemistry · 2011Article
- The structure of the PDZ3-SH3-GuK tandem of ZO-1 protein suggests a supramodular organization of the membrane-associated guanylate kinase (MAGUK) family scaffold protein core.The Journal of biological chemistry · 2011Article
- Homodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.The Journal of biological chemistry · 2011Article
- Allosteric control of regulated scaffolding in membrane-associated guanylate kinases.Biochemistry · 2009Article
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2 authors.
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Abstract
Membrane-associated guanylate kinases (MAGUKs) regulate the formation and function of molecular assemblies at specialized regions of the membrane. Allosteric regulation of an intramolecular interaction between the Src homology 3 (SH3) and guanylate kinase (GK) domains of MAGUKs is thought to play a central role in regulating MAGUK function. Here we show that a mutant of the Drosophila MAGUK Discs large (Dlg), dlg(sw), encodes a form of Dlg that disrupts the intramolecular association while leaving the SH3 and GK domains intact, providing an excellent model system to assess the role of the SH3-GK intramolecular interaction in MAGUK function. Analysis of asymmetric cell division of maternal-zygotic dlg(sw) embryonic neuroblasts demonstrates that the intramolecular interaction is not required for Dlg localization but is necessary for cell fate determinant segregation to the basal cortex and mitotic spindle alignment with the cortical polarity axis. These defects ultimately result in improper patterning of the embryonic central nervous system. Furthermore, we demonstrate that the sw mutation of Dlg results in unregulated complex assembly as assessed by GukHolder association with the SH3-GK versus PDZ-SH3-GK modules of Dlg(sw). From these studies, we conclude that allosteric regulation of the SH3-GK intramolecular interaction is required for regulation of MAGUK function in asymmetric cell division, possibly through regulation of complex assembly.
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