biostudies-literatureLiu PJAmerican Heart AssociationAmerican Society of NephrologyNIDDK NIH HHSNational Institute of Diabetes and Digestive and Kidney Diseases1989-2007https://www.ebi.ac.uk/biostudies/studies/S-EPMC9678034biostudies-literatureUnknown33(11)<h4>Background</h4>Myo1e is a nonmuscle motor protein enriched in podocytes. Mutations in <i>MYO1E</i> are associated with steroid-resistant nephrotic syndrome (SRNS). Most of the <i>MYO1E</i> variants identified by genomic sequencing have not been functionally characterized. Here, we set out to analyze two mutations in the Myo1e motor domain, T119I and D388H, which were selected on the basis of protein sequence conservation.<h4>Methods</h4>EGFP-tagged human <i>Myo1e</i> constructs were delivered into the Myo1e-KO mouse podocyte-derived cells <i>via</i> adenoviral infection to analyze Myo1e protein stability, Myo1e localization, and clathrin-dependent endocytosis, which is known to involve Myo1e activity. Furthermore, truncated <i>Myo1e</i> constructs were expressed using the baculovirus eJournal of the American Society of Nephrology : JASNSteroid-Resistant Nephrotic Syndrome-Associated <i>MYO1E</i> Mutations Have Differential Effects on Myosin 1e Localization, Dynamics, and Activity.PMC9678034R01 DK083345predoctoral fellowship5R01DK076683RC2 DK122397R01 DK07668314PRE20380534Hildebrandt FKrendel MBi-Karchin JPlante ELGunther LKLovric SLiu PJYengo CMGarone MEPerez DPellenz CDPresti MFChase SEZhang CMartin CEfalseSteroid-Resistant Nephrotic Syndrome-Associated <i>MYO1E</i> Mutations Have Differential Effects on Myosin 1e Localization, Dynamics, and Activity.<h4>Background</h4>Myo1e is a nonmuscle motor protein enriched in podocytes. Mutations in <i>MYO1E</i> are associated with steroid-resistant nephrotic syndrome (SRNS). Most of the <i>MYO1E</i> variants identified by genomic sequencing have not been functionally characterized. Here, we set out to analyze two mutations in the Myo1e motor domain, T119I and D388H, which were selected on the basis of protein sequence conservation.<h4>Methods</h4>EGFP-tagged human <i>Myo1e</i> constructs were delivered into the Myo1e-KO mouse podocyte-derived cells <i>via</i> adenoviral infection to analyze Myo1e protein stability, Myo1e localization, and clathrin-dependent endocytosis, which is known to involve Myo1e activity. Furthermore, truncated <i>Myo1e</i> constructs were expressed using the baculovirus e2022-01-01T00:00:00Z2022 Nov2026-05-27T11:08:19.822Z2025-04-04T22:50:14.931ZS-EPMC96780343631609510.1681/ASN.202111150510.1681/asn.2021111505