Tubular lipid binding proteins (TULIPs) growing everywhere☆

Autor: Wong, Louise H., Levine, Tim P.
Jazyk: angličtina
Rok vydání: 2017
Předmět:
E-Syt
extended-synaptotagmin

TULIP
tubular lipid binding protein

SMP
synaptotagmin mitochondria and lipid binding protein

Lipopolysaccharide (LPS)
Tether
PLTP
phospholipid transfer protein

JH
juvenile hormone

JHBP
JH binding protein

Article
LTP
lipid transfer protein

ER
endoplasmic reticulum

Evolution
Molecular

PC
phosphatidylcholine

Bacterial Proteins
DUF
domain of unknown function

Animals
Humans
CFTR
cystic fibrosis transmembrane conductance regulator

LBP
LPS-binding protein

Phospholipid Transfer Proteins
Extended-synaptotagmin (E-Syt)
Binding Sites
ENaC
epithelial sodium channel

ERMES
ER-mitochondrial encounter structure

Anacetrapib
Endoplasmic reticulum-mitochondria encounter structure (ERMES)
LAM
LTP anchored at a membrane contact site

RMSD
root mean square distance

PS
phosphatidylserine

Lipid Metabolism
CETP
cholesterol ester transfer protein

BPI
bacterial permeability-inducing protein

Cholesterol Ester Transfer Proteins
Lipid traffic
DALI
distance matrix alignment

LPS
lipopolysaccharide

lipids (amino acids
peptides
and proteins)

Cystic fibrosis transmembrane conductance regulator (CFTR)
PLUNC
palate lung and nasal epithelial clone

PDZK8
Protein Binding
Zdroj: Biochimica et Biophysica Acta
ISSN: 1878-2434
0006-3002
Popis: Tubular lipid binding proteins (TULIPs) have become a focus of interest in the cell biology of lipid signalling, lipid traffic and membrane contact sites. Each tubular domain has an internal pocket with a hydrophobic lining that can bind a hydrophobic molecule such as a lipid. This allows TULIP proteins to carry lipids through the aqueous phase. TULIP domains were first found in a large family of extracellular proteins related to the bacterial permeability-inducing protein (BPI) and cholesterol ester transfer protein (CETP). Since then, the same fold and lipid transfer capacity have been found in SMP domains (so-called for their occurrence in synaptotagmin, mitochondrial and lipid binding proteins), which localise to intracellular membrane contact sites. Here the methods for identifying known TULIPs are described, and used to find previously unreported TULIPs, one in the silk polymer and another in prokaryotes illustrated by the E. coli protein YceB. The bacterial TULIP alters views on the likely evolution of the domain, suggesting its presence in the last universal common ancestor. The major function of TULIPs is to handle lipids, but we still do not know how they work in detail, or how many more remain to be discovered. This article is part of a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann and Benoit Kornmann.
Highlights • Proteins with the tubular lipid binding fold exist in a wider variety than is usually appreciated. • TULIPs are found in prokaryotes, altering views on their evolution. • It is not yet known whether TULIPs transfer lipids as tunnels or as shuttles. • Tests have not yet been done to say if TULIPs with SMP domains (for example E-syts and ERMES components) tether contact sites. • It is likely that more TULIPs remain to be discovered.
Databáze: OpenAIRE
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