Title: PP2A binds to the LIM domains of Lipoma-Preferred Partner through its PR130/B" subunit to regulate cell adhesion and migration
Authors: Janssens, Veerle ×
Zwaenepoel, Karen
Rossé, Carine
Petit, Marleen
Goris, Jozef
Parker, Peter J #
Issue Date: Apr-2016
Publisher: Co. of Biologists
Series Title: Journal of Cell Science vol:129 issue:8 pages:1605-1618
Article number: jcs.175778
Abstract: Here we identify the LIM protein Lipoma Preferred Partner (LPP) as a novel binding partner of a specific Protein Phosphatase 2A (PP2A) heterotrimer characterised by the regulatory PR130/B"α1 subunit. PR130 interacts with the LIM domains of LPP via a conserved zinc finger-like motif in its differentially spliced N-terminus. Isolated LPP-associated PP2A complexes are catalytically active. PR130 co-localises with LPP at multiple locations within cells, including focal contacts, but is specifically excluded from mature focal adhesions, where LPP is still present. An LPP-PR130 fusion protein only localises to focal adhesions upon deletion of the PR130 PP2A/C-binding domain, suggesting that PR130-LPP complex formation is dynamic, and permanent recruitment of PP2A activity may be unfavourable for focal adhesion maturation. Accordingly, siRNA-mediated knockdown of PR130 increases adhesion of HT1080 fibrosarcoma cells onto collagen I and decreases their migration in scratch wound and transwell assays. Complex formation with LPP is mandatory for these PR130-PP2A functions, as neither phenotype can be rescued by re-expression of a PR130 mutant that no longer binds LPP. Our data highlight the importance of specific, locally recruited PP2A complexes in cell adhesion/migration dynamics.
ISSN: 0021-9533
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Protein Phosphorylation and Proteomics
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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