Sphingolipid transfer proteins defined by the GLTP-fold Journal Article
| Authors: | Malinina, L.; Simanshu, D. K.; Zhai, X.; Samygina, V. R.; Kamlekar, R.; Kenoth, R.; Ochoa-Lizarralde, B.; Malakhova, M. L.; Molotkovsky, J. G.; Patel, D. J.; Brown, R. E. |
| Article Title: | Sphingolipid transfer proteins defined by the GLTP-fold |
| Abstract: | Glycolipid transfer proteins (GLTPs) originally were identified as small (∼24 kDa), soluble, amphitropic proteins that specifically accelerate the intermembrane transfer of glycolipids. GLTPs and related homologs now are known to adopt a unique, helically dominated, two-layer 'sandwich' architecture defined as the GLTP-fold that provides the structural underpinning for the eukaryotic GLTP superfamily. Recent advances now provide exquisite insights into structural features responsible for lipid headgroup selectivity as well as the adaptability of the hydrophobic compartment for accommodating hydrocarbon chains of differing length and unsaturation. A new understanding of the structural versatility and evolutionary premium placed on the GLTP motif has emerged. Human GLTP-motifs have evolved to function not only as glucosylceramide binding/transferring domains for phosphoinositol 4-phosphate adaptor protein-2 during glycosphingolipid biosynthesis but also as selective binding/transfer proteins for ceramide-1-phosphate. The latter, known as ceramide-1-phosphate transfer protein, recently has been shown to form GLTP-fold while critically regulating Group-IV cytoplasmic phospholipase A2 activity and pro-inflammatory eicosanoid production. Copyright © 2015 Cambridge University Press. |
| Journal Title: | Quarterly Reviews of Biophysics |
| Volume: | 48 |
| Issue: | 3 |
| ISSN: | 0033-5835 |
| Publisher: | Cambridge University Press |
| Date Published: | 2015-08-01 |
| Start Page: | 281 |
| End Page: | 322 |
| Language: | English |
| DOI: | 10.1017/s003358351400016x |
| PROVIDER: | scopus |
| PUBMED: | 25797198 |
| PMCID: | PMC4691851 |
| DOI/URL: | |
| Notes: | Export Date: 2 October 2015 -- Source: Scopus |
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