<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Beacham GM</submitter><funding>National Science Foundation graduate research fellowship</funding><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><funding>NIH HHS</funding><pagination>iyac102</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9434228</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>222(1)</volume><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</pubmed_abstract><journal>Genetics</journal><pubmed_title>The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator.</pubmed_title><pmcid>PMC9434228</pmcid><funding_grant_id>R01 GM129325</funding_grant_id><funding_grant_id>R01 GM127548</funding_grant_id><funding_grant_id>DGE-1650441</funding_grant_id><funding_grant_id>S10 OD018516</funding_grant_id><pubmed_authors>Wei DT</pubmed_authors><pubmed_authors>Zheng J</pubmed_authors><pubmed_authors>Camacho MMK</pubmed_authors><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Florens L</pubmed_authors><pubmed_authors>Hollopeter G</pubmed_authors><pubmed_authors>Beyrent E</pubmed_authors><pubmed_authors>Beacham GM</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator.</name><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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2026-07-14T18:53:36.903Z</modification><creation>2024-11-13T10:24:18.353Z</creation></dates><accession>S-EPMC9434228</accession><cross_references><pubmed>35792852</pubmed><doi>10.1093/genetics/iyac102</doi></cross_references></HashMap>