Structural Analysis and Shaping of Plant Endoplasmic Reticulum

The plant endoplasmic reticulum (ER) is a polymorphous network of interconnected membranes found throughout the cell cortex, sandwiched between the plasma membrane and the large tonoplast and contiguous with the nuclear envelope. The plant ER crosses the cell as a membrane bundle, forming trans-vacuolar chains by invagination of the vacuolar membrane, which is normally one or two per cell. At the cell cortex, the structure of the ER network consists of interconverting tubules and cisternae. Similar to other eukaryotes, the tubules and edges of the endoplasmic reticulum cisternae in plants have positive curvature.

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Observation of Endoplasmic Reticulum Structure in Plants

Based on the ability of fluorescent dyes to visualize the ER network in living cells, Lifeasible provides fluorescent protein technology and advanced quantitative imaging technology to observe the structure of plant ER to help uncover the plant-specific mechanisms behind ER structure and dynamics.

Fig.1 The plant ER network forms a reticular structure in the cell cortex. (Brandizzi F., 2021)

Shaping of Endoplasmic Reticulum Structure in Plants

• The ER is a polymorphic network of interconnected membranes that are continuously remodeled as organelles participate in the synthesis of at least one-third of the cellular proteome and essential lipids and are partially triggered by glycans to secrete proteins.
• As cells expand, the ER changes its structure and adjusts its ability to synthesize proteins in response to stress signals that alter the cell's demand for biosynthetic cargoes, including defense proteins.
• We provide insights into the structural shaping of plant ER in terms of gene regulation and the relationship between ER and other organelle structures, including plasmodesmata and actin in the cytoskeleton.

Analysis of Protein Localization in Plant Endoplasmic Reticulum

• After their co-translational insertion into the ER lumen or the ER membrane, most proteins are transported downstream along the secretory pathway via the Golgi. In contrast, a few protein species are retained in the ER. Retention of peptides in the ER is either signal independent or dependent on specific retention signals encoded by the peptide primary sequence.
• We provide research ideas such as signal independent retention in ER, localization signal of soluble ER-resident protein, and retention of whole membrane ER protein to explore protein localization in the plant ER.

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