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Review
. 2022 Dec 13;12(12):1261.
doi: 10.3390/membranes12121261.

The Re-Localization of Proteins to or Away from Membranes as an Effective Strategy for Regulating Stress Tolerance in Plants

Yee-Shan Ku  1 , Sau-Shan Cheng  1 , Ming-Yan Cheung  1 , Cheuk-Hin Law  1 , Hon-Ming Lam  1
Affiliations
Review

The Re-Localization of Proteins to or Away from Membranes as an Effective Strategy for Regulating Stress Tolerance in Plants

Yee-Shan Ku et al. Membranes (Basel). .

Abstract

The membranes of plant cells are dynamic structures composed of phospholipids and proteins. Proteins harboring phospholipid-binding domains or lipid ligands can localize to membranes. Stress perception can alter the subcellular localization of these proteins dynamically, causing them to either associate with or detach from membranes. The mechanisms behind the re-localization involve changes in the lipidation state of the proteins and interactions with membrane-associated biomolecules. The functional significance of such re-localization includes the regulation of molecular transport, cell integrity, protein folding, signaling, and gene expression. In this review, proteins that re-localize to or away from membranes upon abiotic and biotic stresses will be discussed in terms of the mechanisms involved and the functional significance of their re-localization. Knowledge of the re-localization mechanisms will facilitate research on increasing plant stress adaptability, while the study on re-localization of proteins upon stresses will further our understanding of stress adaptation strategies in plants.

Keywords: co-translational modification; myristoylation; palmitoylation; plant stress adaptability; post-translational modification; prenylation; protein lipidation; protein re-localization; transcriptional regulation.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
A diagram illustrating an example of the transcriptional regulations by re-localized proteins upon stress. TMD, transmembrane domain; ORF, open reading frame.
See this image and copyright information in PMC

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