Abstract 2686 Interrogating fibrillin-thylakoid binding mechanics through molecular simulation

Plastoglobules are lipid bodies found on the surface of the thylakoid in photosynthetic organisms. Plastoglobules bud from the thylakoid in response to abiotic stresses. While the morphology of plastoglobules are well established, the mechanism leading to plastoglobule formation and maintenance are unknown. The leading hypothesis is that proteins at the plastoglobule or thylakoid surface drive membrane reorganization leading to plastoglobule budding. In A. thaliana, the protein fibrillin 1A is suspected to bind to plastoglobule membranes to facilitate plastoglobule formation.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.108991
Primary Topic
Cancer, Lipids, and Metabolism
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 2686 Interrogating fibrillin-thylakoid binding mechanics through molecular simulation

A. B. Strong, Josh V. Vermaas, Peter Knut Lundquist, Duncan Boren
Journal of Biological Chemistry
Cancer, Lipids, and Metabolism
article

Abstract 2686 Interrogating fibrillin-thylakoid binding mechanics through molecular simulation

A. B. Strong, Josh V. Vermaas, Peter Knut Lundquist, Duncan Boren
article en

Abstract

Plastoglobules are lipid bodies found on the surface of the thylakoid in photosynthetic organisms. Plastoglobules bud from the thylakoid in response to abiotic stresses. While the morphology of plastoglobules are well established, the mechanism leading to plastoglobule formation and maintenance are unknown. The leading hypothesis is that proteins at the plastoglobule or thylakoid surface drive membrane reorganization leading to plastoglobule budding. In A. thaliana, the protein fibrillin 1A is suspected to bind to plastoglobule membranes to facilitate plastoglobule formation.

Journal of Biological ChemistryVol. 301(5)
Vanderbilt University (US)
Michigan State University, National Institutes of Health, College of Engineering, Michigan State University, National Institute of General Medical Sciences
Openalex Percentile: Top 82%
Cancer, Lipids, and Metabolism
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Abstract 2686 Interrogating fibrillin-thylakoid binding mechanics through molecular simulation — A. B. Strong, Josh V. Vermaas, et al. · Journal of Biological Chemistry (2025) | TGRS Research Map | TGRS