{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ripamonti M"],"funding":["Cancer Research UK"],"pagination":["1025"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9519923"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(1)"],"pubmed_abstract":["Scaffold liprin-α1 is required to assemble dynamic plasma membrane-associated platforms (PMAPs) at the front of migrating breast cancer cells, to promote protrusion and invasion. We show that the N-terminal region of liprin-α1 contains an LxxIxE motif interacting with B56 regulatory subunits of serine/threonine protein phosphatase 2A (PP2A). The specific interaction of B56γ with liprin-α1 requires an intact motif, since two point mutations strongly reduce the interaction. B56γ mediates the interaction of liprin-α1 with the heterotrimeric PP2A holoenzyme. Most B56γ protein is recovered in the cytosolic fraction of invasive MDA-MB-231 breast cancer cells, where B56γ is complexed with liprin-α1. While mutation of the short linear motif (SLiM) does not affect localization of liprin-α1 to PMAPs"],"journal":["Communications biology"],"pubmed_title":["A functional interaction between liprin-α1 and B56γ regulatory subunit of protein phosphatase 2A supports tumor cell motility."],"pmcid":["PMC9519923"],"funding_grant_id":["28159"],"pubmed_authors":["Davey NE","Tonoli D","de Curtis I","Surini S","Lamarca A","Ripamonti M"],"additional_accession":[]},"is_claimable":false,"name":"A functional interaction between liprin-α1 and B56γ regulatory subunit of protein phosphatase 2A supports tumor cell motility.","description":"Scaffold liprin-α1 is required to assemble dynamic plasma membrane-associated platforms (PMAPs) at the front of migrating breast cancer cells, to promote protrusion and invasion. We show that the N-terminal region of liprin-α1 contains an LxxIxE motif interacting with B56 regulatory subunits of serine/threonine protein phosphatase 2A (PP2A). The specific interaction of B56γ with liprin-α1 requires an intact motif, since two point mutations strongly reduce the interaction. B56γ mediates the interaction of liprin-α1 with the heterotrimeric PP2A holoenzyme. Most B56γ protein is recovered in the cytosolic fraction of invasive MDA-MB-231 breast cancer cells, where B56γ is complexed with liprin-α1. While mutation of the short linear motif (SLiM) does not affect localization of liprin-α1 to PMAPs","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-07-14T17:53:20.709Z","creation":"2025-02-19T00:34:59.412Z"},"accession":"S-EPMC9519923","cross_references":{"pubmed":["36171301"],"doi":["10.1038/s42003-022-03989-3"]}}