{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beacham GM"],"funding":["National Science Foundation graduate research fellowship","National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["iyac102"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9434228"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["222(1)"],"pubmed_abstract":["How serine/threonine phosphatases are spatially and temporally tuned by regulatory subunits is a fundamental question in cell biology. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins are protein phosphatase 1 catalytic subunit binding partners associated with cardiocutaneous diseases. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize protein phosphatase 1 catalytic subunit to cell-cell junctions, but how ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize and whether they regulate protein phosphatase 1 catalytic subunit activity in vivo is unclear. Through a Caenorhabditis elegans genetic screen, we find that loss of the ankyrin repeat, SH3 domain, proline-rich-region-containing protein homolog, APE-1, suppresses a pat"],"journal":["Genetics"],"pubmed_title":["The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator."],"pmcid":["PMC9434228"],"funding_grant_id":["R01 GM129325","R01 GM127548","DGE-1650441","S10 OD018516"],"pubmed_authors":["Wei DT","Zheng J","Camacho MMK","Zhang Y","Florens L","Hollopeter G","Beyrent E","Beacham GM"],"additional_accession":[]},"is_claimable":false,"name":"The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator.","description":"How serine/threonine phosphatases are spatially and temporally tuned by regulatory subunits is a fundamental question in cell biology. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins are protein phosphatase 1 catalytic subunit binding partners associated with cardiocutaneous diseases. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize protein phosphatase 1 catalytic subunit to cell-cell junctions, but how ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize and whether they regulate protein phosphatase 1 catalytic subunit activity in vivo is unclear. Through a Caenorhabditis elegans genetic screen, we find that loss of the ankyrin repeat, SH3 domain, proline-rich-region-containing protein homolog, APE-1, suppresses a pat","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-07-14T18:53:36.903Z","creation":"2024-11-13T10:24:18.353Z"},"accession":"S-EPMC9434228","cross_references":{"pubmed":["35792852"],"doi":["10.1093/genetics/iyac102"]}}