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• W3204283060 endingPage "101289" @default.
• W3204283060 startingPage "101289" @default.
• W3204283060 abstract "Scribble, a member of the LAP protein family, contributes to the apicobasal polarity (ABP) of epithelial cells. The LAP-unique region of these proteins, which is essential and sufficient for ABP, includes a conserved Leucine-Rich Repeat (LRR) domain. The major binding partners of this region that could regulate ABP remain unknown. Here, using proteomics, native gel electrophoresis, and site-directed mutagenesis, we show that the concave surface of LRR domain in Scribble participates in three types of mutually exclusive interactions-(i) homodimerization, serving as an auto-inhibitory mechanism; (ii) interactions with a diverse set of polarity proteins, such as Llgl1, Llgl2, EPB41L2, and EPB41L5, which produce distinct multiprotein complexes; and (iii) a direct interaction with the protein phosphatase, PP1. Analogy with the complex between PP1 and LRR domain of SDS22, a well-studied PP1 regulator, suggests that the Scibble-PP1 complex stores a latent form of PP1 in the basolateral cell cortex. Such organization may generate a dynamic signaling network wherein PP1 could be dispatched from the complex with Scribble to particular protein ligands, achieving fast dephosphorylation kinetics." @default.
• W3204283060 created "2021-10-11" @default.
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• W3204283060 date "2021-11-01" @default.
• W3204283060 modified "2023-10-17" @default.
• W3204283060 title "Basolateral protein Scribble binds phosphatase PP1 to establish a signaling network maintaining apicobasal polarity" @default.
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• W3204283060 doi "https://doi.org/10.1016/j.jbc.2021.101289" @default.
• W3204283060 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8569552" @default.
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• W3204283060 hasPublicationYear "2021" @default.
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