{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16"],"submitter":["Heo K"],"funding":["National Institutes of Health","Michael J. Fox Foundation for Parkinson's Research"],"pubmed_abstract":["Microtubule-based transport provides mitochondria to distant regions of neurons and is essential for neuronal health. To identify compounds that increase mitochondrial motility, we screened 1,641 small-molecules in a high-throughput screening platform. Indirubin and cantharidin increased mitochondrial motility in rat cortical neurons. Cantharidin is known to inhibit protein phosphatase 2A (PP2A). We therefore tested two other inhibitors of PP2A: LB-100 and okadaic acid. LB-100 increased mitochondrial motility, but okadaic acid did not. To resolve this discrepancy, we knocked down expression of the catalytic subunit of PP2A (PP2CA). This long-term inhibition of PP2A more than doubled retrograde transport of axonal mitochondria, confirming the importance of PP2A as a regulator of mitochondri"],"journal":["Frontiers in cellular neuroscience"],"pagination":["852245"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8973303"],"repository":["biostudies-literature"],"pubmed_title":["Serine/Threonine Protein Phosphatase 2A Regulates the Transport of Axonal Mitochondria."],"pmcid":["PMC8973303"],"pubmed_authors":["Schwarz TL","Basu H","Gutnick A","Heo K","Wei W","Shlevkov E"],"additional_accession":[]},"is_claimable":false,"name":"Serine/Threonine Protein Phosphatase 2A Regulates the Transport of Axonal Mitochondria.","description":"Microtubule-based transport provides mitochondria to distant regions of neurons and is essential for neuronal health. To identify compounds that increase mitochondrial motility, we screened 1,641 small-molecules in a high-throughput screening platform. Indirubin and cantharidin increased mitochondrial motility in rat cortical neurons. Cantharidin is known to inhibit protein phosphatase 2A (PP2A). We therefore tested two other inhibitors of PP2A: LB-100 and okadaic acid. LB-100 increased mitochondrial motility, but okadaic acid did not. To resolve this discrepancy, we knocked down expression of the catalytic subunit of PP2A (PP2CA). This long-term inhibition of PP2A more than doubled retrograde transport of axonal mitochondria, confirming the importance of PP2A as a regulator of mitochondri","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-26T15:20:40.031Z","creation":"2025-04-06T14:50:53.554Z"},"accession":"S-EPMC8973303","cross_references":{"pubmed":["35370563"],"doi":["10.3389/fncel.2022.852245"]}}