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Sphingolipid transfer proteins defined by the GLTP-fold

Published online by Cambridge University Press:  23 March 2015

Lucy Malinina ,
Dhirendra K. Simanshu ,
Xiuhong Zhai ,
Valeria R. Samygina ,
RaviKanth Kamlekar ,
Roopa Kenoth ,
Borja Ochoa-Lizarralde ,
Margarita L. Malakhova ,
Julian G. Molotkovsky  and
Dinshaw J. Patel
...Show all authors
Lucy Malinina*
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA Structural Biology Unit, CICbioGUNE, Technology Park of Bizkaia, 48160 Derio-Bilbao, Spain
Dhirendra K. Simanshu
Affiliation:
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA
Xiuhong Zhai
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA
Valeria R. Samygina
Affiliation:
Structural Biology Unit, CICbioGUNE, Technology Park of Bizkaia, 48160 Derio-Bilbao, Spain
RaviKanth Kamlekar
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA
Roopa Kenoth
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA
Borja Ochoa-Lizarralde
Affiliation:
Structural Biology Unit, CICbioGUNE, Technology Park of Bizkaia, 48160 Derio-Bilbao, Spain
Margarita L. Malakhova
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA
Julian G. Molotkovsky
Affiliation:
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Dinshaw J. Patel*
Affiliation:
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA
Rhoderick E. Brown*
Affiliation:
The Hormel Institute, University of Minnesota, Austin, MN 55912, USA
*
*Authors for correspondence: Lucy Malinina, Dinshaw J. Patel, Rhoderick E. Brown. E-mails: lucy@hi.umn.edu, pateld@mskcc.org, reb@umn.edu
*Authors for correspondence: Lucy Malinina, Dinshaw J. Patel, Rhoderick E. Brown. E-mails: lucy@hi.umn.edu, pateld@mskcc.org, reb@umn.edu
*Authors for correspondence: Lucy Malinina, Dinshaw J. Patel, Rhoderick E. Brown. E-mails: lucy@hi.umn.edu, pateld@mskcc.org, reb@umn.edu
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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.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 48 , Issue 3 , August 2015 , pp. 281 - 322
Copyright
Copyright © Cambridge University Press 2015 

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Footnotes

†

Present address: Frederick National Laboratory of National Cancer Institute, Frederick, MD, USA.

‡

Present address: Institute of Crystallography RAS, Leninsky pr.59, 119333 Moscow, Russia.

§

Present address: Environmental & Analytical Chemistry Division, School of Advanced Sciences, VIT University, Vellore-632014, TN, India.

References

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