中国物理B ›› 2025, Vol. 34 ›› Issue (5): 58701-058701.doi: 10.1088/1674-1056/adbee9

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Effects of palmitoylation on membrane protein partitioning into lipid domains in model cellular membranes

Shishi Wu(吴施施)1,2 and Qing Liang(梁清)1,2,†   

  1. 1 Department of Physics, Zhejiang Normal University, Jinhua 321004, China;
    2 Zhejiang Institute of Photoelectronics & Zhejiang Institute for Advanced Light Source, Zhejiang Normal University, Jinhua 321004, China
  • 收稿日期:2025-01-31 修回日期:2025-03-05 接受日期:2025-03-11 出版日期:2025-04-18 发布日期:2025-04-24
  • 通讯作者: Qing Liang E-mail:qliang@zjnu.edu.cn
  • 基金资助:
    Project supported by Zhejiang Provincial Natural Science Foundation of China (Grant No. LZ25A040005) and the National Natural Science Foundation of China (Grant No. 11674287).

Effects of palmitoylation on membrane protein partitioning into lipid domains in model cellular membranes

Shishi Wu(吴施施)1,2 and Qing Liang(梁清)1,2,†   

  1. 1 Department of Physics, Zhejiang Normal University, Jinhua 321004, China;
    2 Zhejiang Institute of Photoelectronics & Zhejiang Institute for Advanced Light Source, Zhejiang Normal University, Jinhua 321004, China
  • Received:2025-01-31 Revised:2025-03-05 Accepted:2025-03-11 Online:2025-04-18 Published:2025-04-24
  • Contact: Qing Liang E-mail:qliang@zjnu.edu.cn
  • Supported by:
    Project supported by Zhejiang Provincial Natural Science Foundation of China (Grant No. LZ25A040005) and the National Natural Science Foundation of China (Grant No. 11674287).

摘要: The partitioning of membrane proteins into lipid domains in cellular membranes is closely associated with the realization of the protein functions and it is influenced by various factors such as the post-translational modification of palmitoylation. However, the molecular mechanism of the effect of palmitoylation on membrane protein partitioning into the lipid domains remains elusive. In this work, taking human peripheral myelin protein 22 (PMP22) as an example, we employ coarse-grained molecular dynamics simulations to investigate the partitioning of both the natural PMP22 and the palmitoylated PMP22 (pal-PMP22) into the lipid domains of model myelin membranes. The results indicate that palmitoylation drives PMP22 to localize at the boundary of the liquid-ordered (Lo) and liquid-disordered (Ld) domains and increases the possibility of PMP22 partitioning into the Lo domains by changing the hydrophobic length of the proteins and perturbing the ordered packing of tails of the saturated lipids in the Lo domains. This work offers some novel insights into the role of palmitoylation in modulating the function of membrane proteins in cellular membranes.

关键词: protein, palmitoylation, lipid domain, molecular simulation

Abstract: The partitioning of membrane proteins into lipid domains in cellular membranes is closely associated with the realization of the protein functions and it is influenced by various factors such as the post-translational modification of palmitoylation. However, the molecular mechanism of the effect of palmitoylation on membrane protein partitioning into the lipid domains remains elusive. In this work, taking human peripheral myelin protein 22 (PMP22) as an example, we employ coarse-grained molecular dynamics simulations to investigate the partitioning of both the natural PMP22 and the palmitoylated PMP22 (pal-PMP22) into the lipid domains of model myelin membranes. The results indicate that palmitoylation drives PMP22 to localize at the boundary of the liquid-ordered (Lo) and liquid-disordered (Ld) domains and increases the possibility of PMP22 partitioning into the Lo domains by changing the hydrophobic length of the proteins and perturbing the ordered packing of tails of the saturated lipids in the Lo domains. This work offers some novel insights into the role of palmitoylation in modulating the function of membrane proteins in cellular membranes.

Key words: protein, palmitoylation, lipid domain, molecular simulation

中图分类号:  (Proteins)

  • 87.14.E-
87.15.-v (Biomolecules: structure and physical properties) 87.16.dt (Structure, static correlations, domains, and rafts) 87.15.ap (Molecular dynamics simulation)