ArticleThe Biochemical journal2006
A critical beta6-beta7 loop in the pleckstrin homology domain of ceramide kinase.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 24 citations in OpenAlex.
- Systematic simulation of the interactions of pleckstrin homology domains with membranes.Science advances · 2022Article
- A Nonradioactive Fluorimetric SPE-Based Ceramide Kinase Assay Using NBD-C(6)-Ceramide.Journal of lipids · 2012Article
- A lipid binding domain in sphingosine kinase 2.Biochemical and biophysical research communications · 2009Article
- Ceramide-1-phosphate transfer protein (CPTP) regulation by phosphoinositides.The Journal of biological chemistryArticle
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CerK (ceramide kinase) produces ceramide 1-phosphate, a sphingophospholipid with recognized signalling properties. It localizes to the Golgi complex and fractionates essentially between detergent-soluble and -insoluble fractions; however, the determinants are unknown. Here, we made a detailed mutagenesis study of the N-terminal PH domain (pleckstrin homology domain) of CerK, based on modelling, and identified key positively charged amino acid residues within an unusual motif in the loop interconnecting beta-strands 6 and 7. These residues are critical for CerK membrane association and polyphosphoinositide binding and activity. Their mutagenesis results in increased thermolability, sensitivity to proteolysis, reduced apparent molecular mass as well as propensity of the recombinant mutant protein to aggregate, indicating that this loop impacts the overall conformation of the CerK protein. This is in contrast with most PH domains whose function strongly relies on charges located in the beta1-beta2 loop.
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