<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9</volume><submitter>White-Gloria C</submitter><pubmed_abstract>Lipids are fundamental to the biology of all organisms, including the functioning of subcellular organelles. The plant chloroplast is the site of photosynthesis and serves as a hub of metabolic events that are dynamically regulated between the light and dark periods. The regulation of chloroplast events, like most other biological processes, is often controlled by protein phosphorylation. Here, we explored the lipidome of &lt;i>Arabidopsis thaliana&lt;/i> under both light and dark conditions, examining lipid changes upon overexpression or knockout of the chloroplast-specific phosphatase &lt;i>Shewanella&lt;/i>-like protein phosphatase 1 (SLP1). To date, no substrates have been identified for the phosphatase SLP1. Results indicate that &lt;i>Arabidopsis thaliana&lt;/i> possesses a dynamic lipidome that under</pubmed_abstract><journal>BBA advances</journal><pagination>100180</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12834941</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Lipidomic profiling of Arabidopsis chloroplast protein phosphatase SLP1 mutants reveals altered diurnal lipid remodeling.</pubmed_title><pmcid>PMC12834941</pmcid><pubmed_authors>White-Gloria C</pubmed_authors><pubmed_authors>Moorhead GB</pubmed_authors><pubmed_authors>Buzatto AZ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Lipidomic profiling of Arabidopsis chloroplast protein phosphatase SLP1 mutants reveals altered diurnal lipid remodeling.</name><description>Lipids are fundamental to the biology of all organisms, including the functioning of subcellular organelles. The plant chloroplast is the site of photosynthesis and serves as a hub of metabolic events that are dynamically regulated between the light and dark periods. The regulation of chloroplast events, like most other biological processes, is often controlled by protein phosphorylation. Here, we explored the lipidome of &lt;i>Arabidopsis thaliana&lt;/i> under both light and dark conditions, examining lipid changes upon overexpression or knockout of the chloroplast-specific phosphatase &lt;i>Shewanella&lt;/i>-like protein phosphatase 1 (SLP1). To date, no substrates have been identified for the phosphatase SLP1. Results indicate that &lt;i>Arabidopsis thaliana&lt;/i> possesses a dynamic lipidome that under</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026</publication><modification>2026-06-09T06:53:52.842Z</modification><creation>2026-06-09T03:12:01.365Z</creation></dates><accession>S-EPMC12834941</accession><cross_references><pubmed>41607683</pubmed><doi>10.1016/j.bbadva.2026.100180</doi></cross_references></HashMap>