<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11(7)</volume><submitter>Chen W</submitter><pubmed_abstract>Cell migration plays pivotal roles in many biological processes; however, its underlying mechanism remains unclear. Here, we find that NudC-like protein 2 (NudCL2), a cochaperone of heat shock protein 90 (Hsp90), modulates cell migration by stabilizing both myosin-9 and lissencephaly protein 1 (LIS1). Either knockdown or knockout of NudCL2 significantly increases single-cell migration, but has no significant effect on collective cell migration. Immunoprecipitation-mass spectrometry and western blotting analyses reveal that NudCL2 binds to myosin-9 in mammalian cells. Depletion of NudCL2 not only decreases myosin-9 protein levels, but also results in actin disorganization. Ectopic expression of myosin-9 efficiently reverses defects in actin disorganization and single-cell migration in cells</pubmed_abstract><journal>Cell death &amp; disease</journal><pagination>534</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7360774</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>NudCL2 regulates cell migration by stabilizing both myosin-9 and LIS1 with Hsp90.</pubmed_title><pmcid>PMC7360774</pmcid><pubmed_authors>Liu M</pubmed_authors><pubmed_authors>Zhou T</pubmed_authors><pubmed_authors>Sun X</pubmed_authors><pubmed_authors>Yang C</pubmed_authors><pubmed_authors>Xie S</pubmed_authors><pubmed_authors>Li M</pubmed_authors><pubmed_authors>Liu W</pubmed_authors><pubmed_authors>Wang L</pubmed_authors><pubmed_authors>Zhang W</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>Chen W</pubmed_authors><pubmed_authors>Wang W</pubmed_authors><pubmed_authors>Xu X</pubmed_authors></additional><is_claimable>false</is_claimable><name>NudCL2 regulates cell migration by stabilizing both myosin-9 and LIS1 with Hsp90.</name><description>Cell migration plays pivotal roles in many biological processes; however, its underlying mechanism remains unclear. Here, we find that NudC-like protein 2 (NudCL2), a cochaperone of heat shock protein 90 (Hsp90), modulates cell migration by stabilizing both myosin-9 and lissencephaly protein 1 (LIS1). Either knockdown or knockout of NudCL2 significantly increases single-cell migration, but has no significant effect on collective cell migration. Immunoprecipitation-mass spectrometry and western blotting analyses reveal that NudCL2 binds to myosin-9 in mammalian cells. Depletion of NudCL2 not only decreases myosin-9 protein levels, but also results in actin disorganization. Ectopic expression of myosin-9 efficiently reverses defects in actin disorganization and single-cell migration in cells</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Jul</publication><modification>2025-04-19T21:07:26.782Z</modification><creation>2025-02-19T00:50:54.362Z</creation></dates><accession>S-EPMC7360774</accession><cross_references><pubmed>32665550</pubmed><doi>10.1038/s41419-020-02739-9</doi></cross_references></HashMap>