Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase
The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinos...
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| Published in | The Journal of cell biology Vol. 219; no. 5 |
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| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Rockefeller University Press
04.05.2020
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| Abstract | The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4P), where Stt4 (along with the Sac1 PtdIns4P phosphatase and endoplasmic reticulum–plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function. |
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| AbstractList | The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4P), where Stt4 (along with the Sac1 PtdIns4P phosphatase and endoplasmic reticulum-plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function.The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4P), where Stt4 (along with the Sac1 PtdIns4P phosphatase and endoplasmic reticulum-plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function. Yeast Psd2-catalyzed decarboxylation of phosphatidylserine to phosphatidylethanolamine is activated in a noncanonical mechanism by the Sec14-like phosphatidylinositol-transfer protein Sfh4 via a specific protein–protein interaction, and by Stt4 PtdIns 4-OH kinase–mediated control of phosphatidylserine accessibility to the enzyme. The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4 P ), where Stt4 (along with the Sac1 PtdIns4 P phosphatase and endoplasmic reticulum–plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4 P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function. The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4P), where Stt4 (along with the Sac1 PtdIns4P phosphatase and endoplasmic reticulum-plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function. |
| Author | Eisenberg-Bord, Michal Rodriguez, Martin Man Lam, Sin Bankaitis, Vytas A. Tripathi, Ashutosh Wang, Yaxi Lönnfors, Max Wang, Zehua Lee, Dongju Yuan, Peihua Grabon, Aby Schuldiner, Maya |
| AuthorAffiliation | 3 Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel 1 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 4 University of Chinese Academy of Sciences, Beijing, China 5 State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China 6 Department of Chemistry, Texas A&M University, College Station, TX 2 Department of Molecular & Cellular Medicine, Texas A&M Health Science Center, College Station, TX |
| AuthorAffiliation_xml | – name: 1 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX – name: 6 Department of Chemistry, Texas A&M University, College Station, TX – name: 4 University of Chinese Academy of Sciences, Beijing, China – name: 5 State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China – name: 2 Department of Molecular & Cellular Medicine, Texas A&M Health Science Center, College Station, TX – name: 3 Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel |
| Author_xml | – sequence: 1 givenname: Yaxi orcidid: 0000-0003-3278-6127 surname: Wang fullname: Wang, Yaxi – sequence: 2 givenname: Peihua surname: Yuan fullname: Yuan, Peihua – sequence: 3 givenname: Aby surname: Grabon fullname: Grabon, Aby – sequence: 4 givenname: Ashutosh surname: Tripathi fullname: Tripathi, Ashutosh – sequence: 5 givenname: Dongju surname: Lee fullname: Lee, Dongju – sequence: 6 givenname: Martin surname: Rodriguez fullname: Rodriguez, Martin – sequence: 7 givenname: Max orcidid: 0000-0002-3655-9733 surname: Lönnfors fullname: Lönnfors, Max – sequence: 8 givenname: Michal surname: Eisenberg-Bord fullname: Eisenberg-Bord, Michal – sequence: 9 givenname: Zehua surname: Wang fullname: Wang, Zehua – sequence: 10 givenname: Sin surname: Man Lam fullname: Man Lam, Sin – sequence: 11 givenname: Maya orcidid: 0000-0001-9947-115X surname: Schuldiner fullname: Schuldiner, Maya – sequence: 12 givenname: Vytas A. orcidid: 0000-0002-1654-6759 surname: Bankaitis fullname: Bankaitis, Vytas A. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32303746$$D View this record in MEDLINE/PubMed |
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| Snippet | The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to... Yeast Psd2-catalyzed decarboxylation of phosphatidylserine to phosphatidylethanolamine is activated in a noncanonical mechanism by the Sec14-like... |
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| SubjectTerms | 1-Phosphatidylinositol 4-Kinase - genetics Biological Transport - genetics Cell Metabolism Lipid Metabolism - genetics Membrane Proteins - genetics Metabolism Phosphatidylethanolamines - genetics Phosphatidylethanolamines - metabolism Phosphatidylserines - genetics Phosphatidylserines - metabolism Phospholipid Transfer Proteins - genetics Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics |
| Title | Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase |
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