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• W3209262012 startingPage "235" @default.
• W3209262012 abstract "Proteins often do not function as a single biomolecular entity; instead, they frequently interact with other proteins and biomolecules forming complexes. There is increasing evidence depicting the essentiality of protein-protein interactions (PPIs) governing a wide array of cellular processes. Thus, it is crucial to understand PPIs. Commonly used approaches like genetic (e.g., Yeast Two-Hybrid, Y2H), optical (e.g., Surface Plasmon Resonance, SPR; Fluorescence Resonance Energy Transfer, FRET), and biochemical have rendered ease in developing interactive protein maps as freely available information in protein databases on the web. The underlying basis of traditional protein interaction analysis is the core of biochemical methodologies providing direct evidence of interactions. Co-Immunoprecipitation (Co-IP) is a powerful biochemical technique that facilitates identifying novel interacting partners of a protein of interest in vivo, allowing specific capture of their complexes on an immunoglobulin. Here, using Arf-like (Arl) GTPase-8b (Arl8b) and Pleckstrin Homology Domain-Containing Family M Member 1 (PLEKHM1) as an example of small GTPase-effector pair, we provide a detailed protocol for performing Y2H and Co-IP assays to confirm the interaction between a small GTPase and its effector protein." @default.
• W3209262012 created "2021-11-08" @default.
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• W3209262012 date "2021-01-01" @default.
• W3209262012 modified "2023-10-03" @default.
• W3209262012 title "Methods for binding analysis of small GTP-binding proteins with their effectors" @default.
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• W3209262012 doi "https://doi.org/10.1016/bs.mcb.2021.06.003" @default.
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• W3209262012 hasPublicationYear "2021" @default.
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