Chain Length and Temperature Dependence of the Reversible Association of Model Acylated Proteins with Lipid Bilayers

Pool, Chadler T.; Thompson, T. E.

doi:10.1021/bi980385m

Cited by 41 publications

(53 citation statements)

References 45 publications

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“…Studies involving phospholipid bilayers have nevertheless suggested that single lipid modification does not stably anchor proteins in membranes but rather acts as a facilitator of the interaction (Peitzsch and McLaughlin, 1993;Pool and Thompson, 1998). The strength of the interaction appears to depend on the length of the fatty acid chain (PAL > MYR).…”

Section: Proteins Displaying Only An N-terminal Myred Site: the Plantmentioning

confidence: 99%

Roles of N-Terminal Fatty Acid Acylations in Membrane Compartment Partitioning:Arabidopsis h-Type Thioredoxins as a Case Study

et al. 2013

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N-terminal fatty acylations (N-myristoylation [MYR] and S-palmitoylation [PAL]) are crucial modifications affecting 2 to 4% of eukaryotic proteins. The role of these modifications is to target proteins to membranes. Predictive tools have revealed unexpected targets of these acylations in Arabidopsis thaliana and other plants. However, little is known about how N-terminal lipidation governs membrane compartmentalization of proteins in plants. We show here that h-type thioredoxins (h-TRXs) cluster in four evolutionary subgroups displaying strictly conserved N-terminal modifications. It was predicted that one subgroup undergoes only MYR and another undergoes both MYR and PAL. We used plant TRXs as a model protein family to explore the effect of MYR alone or MYR and PAL in the same family of proteins. We used a high-throughput biochemical strategy to assess MYR of specific TRXs. Moreover, various TRX-green fluorescent protein fusions revealed that MYR localized protein to the endomembrane system and that partitioning between this membrane compartment and the cytosol correlated with the catalytic efficiency of the N-myristoyltransferase acting at the N terminus of the TRXs. Generalization of these results was obtained using several randomly selected Arabidopsis proteins displaying a MYR site only. Finally, we demonstrated that a palmitoylatable Cys residue flanking the MYR site is crucial to localize proteins to micropatching zones of the plasma membrane.

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Section: Proteins Displaying Only An N-terminal Myred Site: the Plantmentioning

confidence: 99%

Roles of N-Terminal Fatty Acid Acylations in Membrane Compartment Partitioning:Arabidopsis h-Type Thioredoxins as a Case Study

et al. 2013

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“…It is well established that attachment of a single myristoyl group to a soluble protein only marginally affects its partitioning affinity for nonpolar (membrane) surfaces [87,88]. Generally, a second acylation event involving palmitate (16 carbons) is needed for soluble proteins to form strong, stable associations with membranes.…”

Section: Gltp Conformational Structurementioning

confidence: 99%

Glycolipid transfer proteins

Brown

Mattjus

2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Glycolipid transfer proteins (GLTPs) are small (24 kD), 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 protein structures of GLTP reveal 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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“…Membrane binding of such lipid-modified proteins is primarily driven by the hydrophobic effect; that is, dehydration of the lipid moiety upon membrane insertion gives rise to a large, favorable change in Gibbs free energy. Hydrophobic burial of an aliphatic chain is accompanied by a change in Gibbs free energy of À3.45 kJ/mol per methylene group (4,5), thus providing a strong driving force for membrane binding of proteins and peptides bearing longchain lipid modifications. However, hydrophobicity is not the only factor at play, because membrane binding is further modulated by electrostatic interactions (most notably, Coulombic attraction to or repulsion from the membrane and polar (de)hydration effects) as well as an entropic penalty incurred when an intrinsically flexible macromolecule binds to a membrane (4)(5)(6)(7).…”

Section: Introductionmentioning

confidence: 99%

“…Hydrophobic burial of an aliphatic chain is accompanied by a change in Gibbs free energy of À3.45 kJ/mol per methylene group (4,5), thus providing a strong driving force for membrane binding of proteins and peptides bearing longchain lipid modifications. However, hydrophobicity is not the only factor at play, because membrane binding is further modulated by electrostatic interactions (most notably, Coulombic attraction to or repulsion from the membrane and polar (de)hydration effects) as well as an entropic penalty incurred when an intrinsically flexible macromolecule binds to a membrane (4)(5)(6)(7). From detailed quantitative thermodynamic analyses of several such interactions (4,8), it has been concluded that at least two lipid modifications are required to tightly anchor a protein to a lipid bilayer membrane such as to reduce the fraction of free protein in the aqueous phase to negligible values (2).…”

Section: Introductionmentioning

confidence: 99%

Structural Thermodynamics of myr-Src(2–19) Binding to Phospholipid Membranes

Scheidt

Klingler

Huster

et al. 2015

Biophysical Journal

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Many proteins are anchored to lipid bilayer membranes through a combination of hydrophobic and electrostatic interactions. In the case of the membrane-bound nonreceptor tyrosine kinase Src from Rous sarcoma virus, these interactions are mediated by an N-terminal myristoyl chain and an adjacent cluster of six basic amino-acid residues, respectively. In contrast with the acyl modifications of other lipid-anchored proteins, the myristoyl chain of Src does not match the host lipid bilayer in terms of chain conformation and dynamics, which is attributed to a tradeoff between hydrophobic burial of the myristoyl chain and repulsion of the peptidic moiety from the phospholipid headgroup region. Here, we combine thermodynamic information obtained from isothermal titration calorimetry with structural data derived from (2)H, (13)C, and (31)P solid-state nuclear magnetic resonance spectroscopy to decipher the hydrophobic and electrostatic contributions governing the interactions of a myristoylated Src peptide with zwitterionic and anionic membranes made from lauroyl (C12:0) or myristoyl (C14:0) lipids. Although the latter are expected to enable better hydrophobic matching, the Src peptide partitions more avidly into the shorter-chain lipid analog because this does not require the myristoyl chain to stretch extensively to avoid unfavorable peptide/headgroup interactions. Moreover, we find that Coulombic and intrinsic contributions to membrane binding are not additive, because the presence of anionic lipids enhances membrane binding more strongly than would be expected on the basis of simple Coulombic attraction.

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Chain Length and Temperature Dependence of the Reversible Association of Model Acylated Proteins with Lipid Bilayers

Cited by 41 publications

References 45 publications

Roles of N-Terminal Fatty Acid Acylations in Membrane Compartment Partitioning:Arabidopsis h-Type Thioredoxins as a Case Study

Roles of N-Terminal Fatty Acid Acylations in Membrane Compartment Partitioning:Arabidopsis h-Type Thioredoxins as a Case Study

Glycolipid transfer proteins

Structural Thermodynamics of myr-Src(2–19) Binding to Phospholipid Membranes

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