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AP-MS of MAGU-2 in the nematode C. elegans

ABSTRACT: The Crumbs complex is a regulator of epithelial polarity and is important for the formation of the apical domain. The Crumbs complex consists of the Crumbs protein, Pals1, and PATJ. In C. elegans, we identify MAGU-2 as an ortholog of Pals1. We find that MAGU-2 localizes apically in epithelial cells and its localization is dependent on Crumbs. AP-MS was performed on animals endogenously expressing MAGU-2::GFP and four control strains to identify interactors of MAGU-2. From the data, we identify MPZ-1 as the top hit and identify it as the C. elegans ortholog of PATJ.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Caenorhabditis Elegans

SUBMITTER: Jason Kroll

LAB HEAD: Mike Boxem

PROVIDER: PXD030122 | Pride | 2022-05-19

REPOSITORIES: Pride

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Identification and characterization of Crumbs polarity complex proteins in Caenorhabditis elegans.

Castiglioni Victoria G VG Ramalho João J JJ Kroll Jason R JR Stucchi Riccardo R van Beuzekom Hanna H Schmidt Ruben R Altelaar Maarten M Boxem Mike M

The Journal of biological chemistry 20220303 4

Crumbs proteins are evolutionarily conserved transmembrane proteins with essential roles in promoting the formation of the apical domain in epithelial cells. The short intracellular tail of Crumbs proteins are known to interact with several proteins, including the scaffolding protein PALS1 (protein associated with LIN7, Stardust in Drosophila). PALS1 in turn binds to a second scaffolding protein PATJ (PALS1-associated tight junction protein) to form the core Crumbs/PALS1/PATJ complex. While esse ...[more]

PMID: 35247383

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