ArticleEMBO reports2019
PPM1G forms a PPP-type phosphatase holoenzyme with B56δ that maintains adherens junction integrity.
Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Integrative phosphoproteomic analysis reveals co-regulatory phosphorylation networks of rhotekin in cancer progression.Discover oncology · 2026Article
- Overexpression ofTranslational lung cancer research · 2025Article
- PPM1G and its diagnostic, prognostic and therapeutic potential in HCC (Review).International journal of oncology · 2024Review
- PPM1G dephosphorylates eIF4E in control of mRNA translation and cell proliferation.Life science alliance · 2024Article
- Identification of Potentially Novel Molecular Targets of Endometrial Cancer Using a Non-Biased Proteomic Approach.Cancers · 2023Article
- Prognostic and immunological potential of PPM1G in lung adenocarcinoma.Molecular medicine reports · 2023Article
- PPP2R5D promotes hepatitis C virus infection by binding to viral NS5B and enhancing viral RNA replication.Virology journal · 2022Article
- High expression of PPM1G is associated with the progression and poor prognosis of hepatocellular carcinoma.Cancer biomarkers : section A of Disease markers · 2022Article
- Clinical Value of PPM1G Gene in Survival Prognosis and Immune Infiltration of Hepatocellular Carcinoma.Applied bionics and biomechanics · 2022Article
- Protein phosphatase 2A - structure, function and role in neurodevelopmental disorders.Journal of cell science · 2021Review
- Protein phosphatases in TLR signaling.Cell communication and signaling : CCS · 2021Review
- Reduction of protein phosphatase 2A (PP2A) complexity reveals cellular functions and dephosphorylation motifs of the PP2A/B'δ holoenzyme.The Journal of biological chemistry · 2020Article
- PPM1G forms a PPP-type phosphatase holoenzyme with B56δ that maintains adherens junction integrity.EMBO reports · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Serine/threonine phosphatases achieve substrate diversity by forming distinct holoenzyme complexes in cells. Although the PPP family of serine/threonine phosphatase family members such as PP1 and PP2A are well known to assemble and function as holoenzymes, none of the PPM family members were so far shown to act as holoenzymes. Here, we provide evidence that PPM1G, a member of PPM family of serine/threonine phosphatases, forms a distinct holoenzyme complex with the PP2A regulatory subunit B56δ. B56δ promotes the re-localization of PPM1G to the cytoplasm where the phosphatase can access a discrete set of substrates. Further, we unveil α-catenin, a component of adherens junction, as a new substrate for the PPM1G-B56 phosphatase complex in the cytoplasm. B56δ-PPM1G dephosphorylates α-catenin at serine 641, which is necessary for the appropriate assembly of adherens junctions and the prevention of aberrant cell migration. Collectively, we reveal a new holoenzyme with PPM1G-B56δ as integral components, in which the regulatory subunit provides accessibility to distinct substrates for the phosphatase by defining its cellular localization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.