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- W2290084890 abstract "PSD-95/Dlg/ZO-1 (PDZ) domains are protein-protein interaction modules that generally interact with the C-terminus of partner scaffold proteins to participate in signal transduction processes. A subset of PDZ domains also interact with phophoinositides (PtdIns) and/or cholesterol. Our study focuses on the calcium/calmodulin-dependent serine protein kinase (CASK) PDZ domain that has been shown to synergistically interact with both protein binding partners and PtdIns. First, we quantitate the interaction between the CASK PDZ domain and known interaction partners. We show that the CASK PDZ domain binds to neurexin1 (NRXN1) and phosphorylated syndecan1 (pSDC1) with micromolar affinity, and only weakly (>100 μM) with unphosphorylated syndecan isoforms (SDC1-4). Second, we determined the crystal structure of the CASK PDZ domain alone and complexed with several peptides. A comparison of the CASK PDZ/NRXN1 structure with the CASK PDZ/SDC structures indicates that peptide-binding shifts the α2-helix adjacent to the binding pocket resulting in a more expanded binding groove. Moreover, the CASK/pSDC1 crystal structure shows an interaction between residue R517 and the phosphoryl group of pSDC1, suggesting that his new feature provides specificity and affinity. Consistent with previous literature, protein-lipid blot analysis data showed that the CASK PDZ binds to various PtdIns molecules. However, NMR-based titration data indicated that this interaction is weak. Future experiments will explore the cooperativity of peptides and PtdIns in binding the CASK PDZ in the context of cell membranes." @default.
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- W2290084890 date "2016-02-01" @default.
- W2290084890 modified "2023-09-30" @default.
- W2290084890 title "Structural and Biochemical Characterization of CASK PDZ Interaction with Protein and Lipid Binding Partners" @default.
- W2290084890 doi "https://doi.org/10.1016/j.bpj.2015.11.296" @default.
- W2290084890 hasPublicationYear "2016" @default.
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