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Detection of Lipid-Bound Bacteriorhodopsin Trimer Complex Directly from Purple Membrane by Native Mass Spectrometry
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Evaluation of Surface-Induced Dissociation Ion Mobility-Mass Spectrometry for Lipid Structural Characterization
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A lipid gating mechanism for the channel-forming O antigen ABC transporter
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Discovery, structure and mechanism of a tetraether lipid synthase
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Exogenous lipid vesicles induce endocytosis-mediated cellular aggregation via filopodia retraction in a close unicellular relative of animals
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Penetration and preferential binding of charged nanoparticles to mixed lipid monolayers: interplay o
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Ethylene oxide graft copolymers reduce the immunogenicity of lipid nanoparticles
LNPs made with the polyamide PGE have low immunogenicity and outperform PEG-LNPs after chronic administration.
The mosquito protein AEG12 displays both cytolytic and antiviral properties via a common lipid trans
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Reply to Nagle et al.: The universal stiffening effects of cholesterol on lipid membranes
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A proteoliposome-based system reveals how lipids control photosynthetic light harvesting
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The mitochondria-targeted peptide SS-31 binds lipid bilayers and modulates surface electrostatics as a key component of its mechanism of action
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A conserved evolutionary mechanism permits Δ9 desaturation of very-long-chain fatty acyl lipids
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VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
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Structural and biochemical insights into lipid transport by VPS13 proteins
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Plant and Algal Lipids: In All Their States and on All Scales
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PII interactions with the acetyl-CoA carboxylase subunits BADC and BCCP co-regulate lipid and nitrogen metabolism in Arabidopsis
In plants, the initiation of fatty acid synthesis is catalyzed by acetyl-CoA carboxylase (ACCase), which produces malonyl-CoA. The heteromeric form of ACCase (htACCase) is a holoenzyme consisting of biotin carboxylase and carboxyltransferase sub-complexes, both of which are subject to extensive regulation. Biotin carboxylase activity is controlled in part by the presence of the catalytic biotin carboxyl carrier proteins (BCCP1/2) and/or the non-catalytic, non-biotinylated, biotin/lipoyl attachment domain-containing proteins (BADC1/2/3) that associate with backbone biotin carboxylase (BC) protein. However, the mechanisms regulating BADC and BCCP interactions with BC and, consequently, ACCase activity in planta , remain unclear. Here, we demonstrate that the Arabidopsis ( Arabidopsis thaliana ) regulatory protein PII modulates htACCase activity through independent interactions with BADC and BCCP proteins in a selective manner. Analysis of badc1 badc2 and badc1 badc3 mutant lines and the respective pii triple mutants revealed that changes in seed oil and protein accumulation of badc double mutants are PII/nitrogen dependent. Absolute quantification of htACCase subunits and PII in developing seeds suggests that Arabidopsis exerts tight regulation over individual protein stoichiometry to balance oil and protein accumulation. The effects on vegetative and seed development indicate that PII and BADC proteins have distinct yet overlapping roles in regulating plant metabolism.