Protein kinase D (PKD) has been identified as a crucial regulator of secretory transport at the trans-Golgi network (TGN). Recruitment and activation of PKD at the TGN is mediated by the lipid diacylglycerol, a pool of which is generated by sphingomyelin synthase from ceramide and phosphatidylcholine. The nonvesicular transfer of ceramide from the endoplasmic reticulum to the Golgi complex is mediated by the lipid transfer protein CERT (ceramide transport). In this study, we identify CERT as a novel in vivo PKD substrate. Phosphorylation on serine 132 by PKD decreases the affinity of CERT toward its lipid target phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity, identifying PKD as a regulator of lipid homeostasis. We also show that CERT, in turn, is critical for PKD activation and PKD-dependent protein cargo transport to the plasma membrane. Thus, the interdependence of PKD and CERT is key to the maintenance of Golgi membrane integrity and secretory transport.
%0 Journal Article
%1 Fugmann2007
%A Fugmann, Tim
%A Hausser, Angelika
%A Schöffler, Patrik
%A Schmid, Simone
%A Pfizenmaier, Klaus
%A Olayioye, Monilola A.
%D 2007
%J Journal of Cell Biology
%K 2007 hausser izi olayioye pfizenmaier
%N 1
%P 15--22
%R 10.1083/jcb.200612017
%T Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
%U https://www.ncbi.nlm.nih.gov/pubmed/17591919
%V 178
%X Protein kinase D (PKD) has been identified as a crucial regulator of secretory transport at the trans-Golgi network (TGN). Recruitment and activation of PKD at the TGN is mediated by the lipid diacylglycerol, a pool of which is generated by sphingomyelin synthase from ceramide and phosphatidylcholine. The nonvesicular transfer of ceramide from the endoplasmic reticulum to the Golgi complex is mediated by the lipid transfer protein CERT (ceramide transport). In this study, we identify CERT as a novel in vivo PKD substrate. Phosphorylation on serine 132 by PKD decreases the affinity of CERT toward its lipid target phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity, identifying PKD as a regulator of lipid homeostasis. We also show that CERT, in turn, is critical for PKD activation and PKD-dependent protein cargo transport to the plasma membrane. Thus, the interdependence of PKD and CERT is key to the maintenance of Golgi membrane integrity and secretory transport.
%Z Fugmann, TimHausser, AngelikaSchoffler, PatrikSchmid, SimonePfizenmaier, KlausOlayioye, Monilola AengResearch Support, Non-U.S. Gov'tJ Cell Biol. 2007 Jul 2;178(1):15-22. doi: 10.1083/jcb.200612017. Epub 2007 Jun 25.
%7 2007/06/27
%@ 0021-9525 (Print)$\backslash$r0021-9525 (Linking)
@article{Fugmann2007,
abstract = {Protein kinase D (PKD) has been identified as a crucial regulator of secretory transport at the trans-Golgi network (TGN). Recruitment and activation of PKD at the TGN is mediated by the lipid diacylglycerol, a pool of which is generated by sphingomyelin synthase from ceramide and phosphatidylcholine. The nonvesicular transfer of ceramide from the endoplasmic reticulum to the Golgi complex is mediated by the lipid transfer protein CERT (ceramide transport). In this study, we identify CERT as a novel in vivo PKD substrate. Phosphorylation on serine 132 by PKD decreases the affinity of CERT toward its lipid target phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity, identifying PKD as a regulator of lipid homeostasis. We also show that CERT, in turn, is critical for PKD activation and PKD-dependent protein cargo transport to the plasma membrane. Thus, the interdependence of PKD and CERT is key to the maintenance of Golgi membrane integrity and secretory transport.},
added-at = {2023-06-29T13:07:55.000+0200},
annote = {Fugmann, TimHausser, AngelikaSchoffler, PatrikSchmid, SimonePfizenmaier, KlausOlayioye, Monilola AengResearch Support, Non-U.S. Gov'tJ Cell Biol. 2007 Jul 2;178(1):15-22. doi: 10.1083/jcb.200612017. Epub 2007 Jun 25.},
author = {Fugmann, Tim and Hausser, Angelika and Sch{\"{o}}ffler, Patrik and Schmid, Simone and Pfizenmaier, Klaus and Olayioye, Monilola A.},
biburl = {https://puma.ub.uni-stuttgart.de/bibtex/24c9f5da9529f7feb43d02eee34cf053c/fabian},
doi = {10.1083/jcb.200612017},
edition = {2007/06/27},
interhash = {679c72b8dd58f26768d8fe98fac798ca},
intrahash = {4c9f5da9529f7feb43d02eee34cf053c},
isbn = {0021-9525 (Print)$\backslash$r0021-9525 (Linking)},
issn = {00219525},
journal = {Journal of Cell Biology},
keywords = {2007 hausser izi olayioye pfizenmaier},
number = 1,
pages = {15--22},
pmid = {17591919},
timestamp = {2023-06-29T13:07:55.000+0200},
title = {{Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein}},
url = {https://www.ncbi.nlm.nih.gov/pubmed/17591919},
volume = 178,
year = 2007
}