Molecular Mechanism of Lipid Recognition and Membrane-Guided Gating in Plant Minimal START Proteins
Kumari, K.; Mahtha, S. K.; Parihar, M.; Tiwari, G.; Yadav, G.; Gaur, V. · biochemistry · 2026-09-07 · 原文
DOI：10.64898/2026.07.22.740216作者：6 位
The hydrophobic nature of lipids requires specialized transport mechanisms, and one such non-vesicular transport mechanism involves START (StAR-related lipid transfer) domain proteins. START domains either occur as a part of multidomain proteins or occur solo as in minimal START proteins. Unlike well-studied multidomain variants, plant minimal START proteins remain poorly understood, leaving their ligand specificity, structural dynamics, and biological roles largely uncharacterized. Integrating structural screening with experimental validation, we analyzed representative plant minimal START proteins and confirmed their specific binding to amphipathic lipids, primarily myristic acid and lysophosphatidylcholine. The ligand binding involves a bipartite mechanism, in which basic residues within the cavity interact with polar lipid headgroups, while the hydrophobic tails are accommodated deeper within the cavity. Mechanistically, ligand binding induced closure of a lid-like gate at the cavity entrance, whereas membrane proximity promoted reopening of the gate and ligand release, collectively suggesting a membrane-guided gating mechanism for lipid exchange. Consistent with this model, lo
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1. 人话版
The hydrophobic nature of lipids requires specialized transport mechanisms, and one such non-vesicular transport mechanism involves START (StAR-related lipid transfer) domain proteins.
START domains either occur as a part of multidomain proteins or occur solo as in minimal START proteins.
2. 领域脉络
本文类目：biochemistry，属于其所在研究脉络的最新进展。
3. 机制拆解
Unlike well-studied multidomain variants, plant minimal START proteins remain poorly understood, leaving their ligand specificity, structural dynamics, and biological roles largely uncharacterized.
Integrating structural screening with experimental validation, we analyzed representative plant minimal START proteins and confirmed their specific binding to amphipathic lipids, primarily myristic acid and lysophosphatidylcholine.
The ligand binding involves a bipartite mechanism, in which basic residues within the cavity interact with polar lipid headgroups, while the hydrophobic tails are accommodated deeper within the cavity.
4. 证据与数字
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5. 反例与边界
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8. 术语表
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