Glycolipid transfer proteins

Rhoderick E. Brown; Peter Mattjus

doi:10.1016/j.bbalip.2007.01.011

Glycolipid transfer proteins

Rhoderick E. Brown, Peter Mattjus

Hormel Institute

Research output: Contribution to journal › Review article › peer-review

71 Scopus citations

Abstract

Glycolipid transfer proteins (GLTPs) are small (24 kDa), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid- and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D architecture of GLTP reveals liganded structures with unique lipid-binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid-binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.

Original language	English (US)
Pages (from-to)	746-760
Number of pages	15
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	1771
Issue number	6
DOIs	https://doi.org/10.1016/j.bbalip.2007.01.011
State	Published - Jun 2007

Bibliographical note

Funding Information:
We wish to express our gratitude to former and present members of the REB and PM laboratories. Special thanks to Dinshaw J. Patel (Memorial Sloan Kettering Cancer Center) for the essential collaborative contributions enabling elucidation of GLTP structure as Co-PI of NIH/NCI CA121493, to Lucy Malinina for leading contributions in solving the structure of GLTP, and to Julian G. Molotkovsky (Shemyakin-Ovhininnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences) for synthesizing many of the sphingolipid fluorophores used to investigate GLTPs over the past decade. Financial support: REB, United States Public Health Service (NIH-GM45928 & NIH-CA121493) and the Hormel Foundation; PM, Academy of Finland, Sigrid Jusélius Foundation, Magnus Ehrnrooth Foundation, Svenska Kulturfonden, Medicinska Understödsföreningen Liv och Hälsa r.f., and Åbo Akademi University.

Keywords

ACD11
Cerebroside
Cholesterol
FAPP2
GLTP
Ganglioside
Glycosphingolipid
HET-C2
Lipid transfer protein structure
Membrane interaction motif
Phosphatidylcholine
Sphingomyelin

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title = "Glycolipid transfer proteins",

abstract = "Glycolipid transfer proteins (GLTPs) are small (24 kDa), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid- and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D architecture of GLTP reveals liganded structures with unique lipid-binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid-binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.",

keywords = "ACD11, Cerebroside, Cholesterol, FAPP2, GLTP, Ganglioside, Glycosphingolipid, HET-C2, Lipid transfer protein structure, Membrane interaction motif, Phosphatidylcholine, Sphingomyelin",

author = "Brown, {Rhoderick E.} and Peter Mattjus",

note = "Funding Information: We wish to express our gratitude to former and present members of the REB and PM laboratories. Special thanks to Dinshaw J. Patel (Memorial Sloan Kettering Cancer Center) for the essential collaborative contributions enabling elucidation of GLTP structure as Co-PI of NIH/NCI CA121493, to Lucy Malinina for leading contributions in solving the structure of GLTP, and to Julian G. Molotkovsky (Shemyakin-Ovhininnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences) for synthesizing many of the sphingolipid fluorophores used to investigate GLTPs over the past decade. Financial support: REB, United States Public Health Service (NIH-GM45928 & NIH-CA121493) and the Hormel Foundation; PM, Academy of Finland, Sigrid Jus{\'e}lius Foundation, Magnus Ehrnrooth Foundation, Svenska Kulturfonden, Medicinska Underst{\"o}dsf{\"o}reningen Liv och H{\"a}lsa r.f., and {\AA}bo Akademi University. ",

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AU - Mattjus, Peter

N1 - Funding Information: We wish to express our gratitude to former and present members of the REB and PM laboratories. Special thanks to Dinshaw J. Patel (Memorial Sloan Kettering Cancer Center) for the essential collaborative contributions enabling elucidation of GLTP structure as Co-PI of NIH/NCI CA121493, to Lucy Malinina for leading contributions in solving the structure of GLTP, and to Julian G. Molotkovsky (Shemyakin-Ovhininnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences) for synthesizing many of the sphingolipid fluorophores used to investigate GLTPs over the past decade. Financial support: REB, United States Public Health Service (NIH-GM45928 & NIH-CA121493) and the Hormel Foundation; PM, Academy of Finland, Sigrid Jusélius Foundation, Magnus Ehrnrooth Foundation, Svenska Kulturfonden, Medicinska Understödsföreningen Liv och Hälsa r.f., and Åbo Akademi University.

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N2 - Glycolipid transfer proteins (GLTPs) are small (24 kDa), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid- and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D architecture of GLTP reveals liganded structures with unique lipid-binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid-binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.

AB - Glycolipid transfer proteins (GLTPs) are small (24 kDa), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid- and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D architecture of GLTP reveals liganded structures with unique lipid-binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid-binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.

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KW - HET-C2

KW - Lipid transfer protein structure

KW - Membrane interaction motif

KW - Phosphatidylcholine

KW - Sphingomyelin

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DO - 10.1016/j.bbalip.2007.01.011

M3 - Review article

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SN - 1388-1981

VL - 1771

SP - 746

EP - 760

JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

IS - 6

ER -

Glycolipid transfer proteins

Abstract

Bibliographical note

Keywords

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