ArticlePloS one2013
Crystal structure of the pleckstrin homology domain from the ceramide transfer protein: implications for conformational change upon ligand binding.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- The C10orf76-PI4KB axis orchestrates CERT-mediated ceramide trafficking to the distal Golgi.The Journal of cell biology · 2023Article
- CERT1 mutations perturb human development by disrupting sphingolipid homeostasis.The Journal of clinical investigation · 2023Article
- Function of ceramide transfer protein for biogenesis and sphingolipid composition of extracellular vesicles.Journal of extracellular vesicles · 2022Article
- Ceramide Transfer Protein (CERT): An Overlooked Molecular Player in Cancer.International journal of molecular sciences · 2021Review
- Ceramide analog [Scientific reports · 2020Article
- Emerging roles for human glycolipid transfer protein superfamily members in the regulation of autophagy, inflammation, and cell death.Progress in lipid research · 2020Review
- Identification of the Interactions Interference Between the PH and START Domain of CERT by Limonoid and HPA Inhibitors.Frontiers in molecular biosciences · 2020Article
- CNature communications · 2018Article
- Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites.Journal of lipid research · 2018Review
- Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif.The Journal of biological chemistry · 2018Article
- Interaction between the PH and START domains of ceramide transfer protein competes with phosphatidylinositol 4-phosphate binding by the PH domain.The Journal of biological chemistry · 2017Article
- Computational Analysis of the Binding Specificities of PH Domains.BioMed research international · 2015Article
- Cellular and molecular interactions of phosphoinositides and peripheral proteins.Chemistry and physics of lipids · 2014Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ceramide transfer protein (CERT) is responsible for the nonvesicular trafficking of ceramide from the endoplasmic reticulum (ER) to the trans Golgi network where it is converted to sphingomyelin (SM). The N-terminal pleckstrin homology (PH) domain is required for Golgi targeting of CERT by recognizing the phosphatidylinositol 4-phosphate (PtdIns(4)P) enriched in the Golgi membrane. We report a crystal structure of the CERT PH domain. This structure contains a sulfate that is hydrogen bonded with residues in the canonical ligand-binding pocket of PH domains. Our nuclear magnetic resonance (NMR) chemical shift perturbation (CSP) analyses show sulfate association with CERT PH protein resembles that of PtdIns(4)P, suggesting that the sulfate bound structure likely mimics the holo form of CERT PH protein. Comparison of the sulfate bound structure with the apo form solution structure shows structural rearrangements likely occur upon ligand binding, suggesting conformational flexibility in the ligand-binding pocket. This structural flexibility likely explains CERT PH domain's low affinity for PtdIns(4)P, a property that is distinct from many other PH domains that bind to their phosphoinositide ligands tightly. This unique structural feature of CERT PH domain is probably tailored towards the transfer activity of CERT protein where it needs to shuttle between ER and Golgi and therefore requires short resident time on ER and Golgi membranes.
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