Summary of study ST001859

This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench,, where it has been assigned Project ID PR001172. The data can be accessed directly via it's Project DOI: 10.21228/M86T2S This work is supported by NIH grant, U2C- DK119886.


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Study IDST001859
Study TitledTor affects the fat body lipidome via Nep1r1, Ctdnep1 and Lipin
Study SummaryQuantitative MS analysis was performed on ten 4 day-old Drosophila larval fat bodies homogenized in 50µl D-PBS (Dulbecco’s Phosphate Buffered Saline without Mg2+ and Ca2+) by Lipotype using previously described methods (Grillet et al, 2016).
VIB KULeuven
DepartmentDept. of Neurosciences, KU Leuven, 3000 Leuven, Belgium
Last NameJacquemyn
First NameJulie
AddressON 4, 6e verd Campus Gasthuisberg, Herestraat 49, bus 602, Leuven, NA, 3000, Belgium
Submit Date2021-06-22
Analysis Type DetailLC-MS
Release Date2021-07-18
Release Version1
Julie Jacquemyn Julie Jacquemyn application/zip

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Project ID:PR001172
Project DOI:doi: 10.21228/M86T2S
Project Title:Torsin and NEP1R1-CTDNEP1 affect interphase NPC insertion by lipid-dependent and -independent mechanisms
Project Type:MS analysis performed by Lipotype on Drosophila larval fat body tissue
Project Summary:The interphase nuclear envelope is extensively remodeled during nuclear pore complex insertion. The process is relatively poorly understood, including why it requires the Torsin ATPases that also regulate NE-localized lipid metabolism. Here we show that fly dTorsin affects lipid metabolism through the NEP1R1-CTDNEP1 phosphatase/ Lipin phosphatidic acid phosphatase pathway. At a cellular level, fly and mouse Torsins removed NEP1R1-CTDNEP1 from the NE to, in turn, exclude Lipin from the nucleus. NEP1R1-CTDNEP1 downregulation also restored nuclear pore membrane fusion in post-mitotic dTorsinKO fat body cells. However, Lipin downregulation was ineffective and membrane fusion defects did not correlate with lipidomic abnormalities. Further testing confirmed that membrane fusion continued in cells with excess Lipin function. It also led to the surprising finding that excess PA metabolism inhibited recruitment of the inner ring complex Nup35 subunit, resulting in elongated channel-like structures in place of mature nuclear pores. We conclude that the NEP1R1-CTDNEP1 phosphatase affects interphase NPC biogenesis by lipid-dependent and lipid-independent mechanisms and this explains some of the pleiotropic effects of Torsins.
Institute:VIB KULeuven
Department:Dept. of Neurosciences, KU Leuven, 3000 Leuven, Belgium
Last Name:Jacquemyn
First Name:Julie
Address:ON 4, 6e verd Campus Gasthuisberg, Herestraat 49, bus 602, 3000 Leuven, Belgium