[HTML][HTML] Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif
Sphingolipids such as ceramide are important constituents of cell membranes. The
ceramide transfer protein (CERT) moves ceramide from the endoplasmic reticulum to the
Golgi apparatus in a nonvesicular manner. Hyperphosphorylation of the serine-repeat motif
(SRM) adjacent to the pleckstrin homology (PH) domain of CERT down-regulates the inter-
organelle ceramide transport function of CERT. However, the mechanistic details of this
down-regulation remain elusive. Using solution NMR and binding assays, we herein show …
ceramide transfer protein (CERT) moves ceramide from the endoplasmic reticulum to the
Golgi apparatus in a nonvesicular manner. Hyperphosphorylation of the serine-repeat motif
(SRM) adjacent to the pleckstrin homology (PH) domain of CERT down-regulates the inter-
organelle ceramide transport function of CERT. However, the mechanistic details of this
down-regulation remain elusive. Using solution NMR and binding assays, we herein show …