Osmotic shock-dependent redistribution of diacylglycerol kinase η1 to non-ionic detergent-resistant membrane via pleckstrin homology and C1 domains
Journal of Biochemistry, ISSN: 0021-924X, Vol: 153, Issue: 2, Page: 179-190
2013
- 9Citations
- 10Captures
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Metrics Details
- Citations9
- Citation Indexes9
- CrossRef8
- Captures10
- Readers10
- 10
Article Description
Diacylglycerol kinase (DGK) participates in regulating the intracellular concentrations of two bioactive lipids, diacylglycerol and phosphatidic acid. DGKη1 is a type II isozyme that contains a pleckstrin homology (PH) domain and a pair of C1 domains at the N-terminus and separated catalytic domains (catalytic subdomain-a and b). We previously reported that DGKη1 expressed in COS-7 cells is translocated from the cytoplasm to punctate granules that partially include endosomes in response to stress stimuli such as osmotic shock. However, the biochemical properties of the stress-dependent behaviour of DGKη1 remain unknown. Here, we have found that DGKη1 is redistributed from the cytosol to the non-ionic detergent (Nonidet P-40)-resistant membrane (DRM) in response to osmotic shock. Our results strongly suggested that the Nonidet P-40 insolubility of DGKη1 is due to neither cytoskeleton localization nor lipid raft association, implying that DGKη1 is distributed to detergent-resistant membrane microdomains that have a low lipid-to-protein ratio. We revealed, using a series of DGKη1 deletion mutants, that the PH and C1 domains play a pivotal role in osmotic shock-dependent DRM redistribution, whereas catalytic subdomain-a negatively regulates the event. © The Authors 2012. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84878198484&origin=inward; http://dx.doi.org/10.1093/jb/mvs130; http://www.ncbi.nlm.nih.gov/pubmed/23127959; https://academic.oup.com/jb/article-lookup/doi/10.1093/jb/mvs130; https://dx.doi.org/10.1093/jb/mvs130; https://academic.oup.com/jb/article-abstract/153/2/179/824021?redirectedFrom=fulltext
Oxford University Press (OUP)
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