ArticleFrontiers in cell and developmental biology2020
Self-Association of Purified Reconstituted ER Luminal Spacer Climp63.
Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress.bioRxiv : the preprint server for biology · 2026Article
- Qa-SNARE syntaxin 18 mediates lipid droplet fusion with SNAP23 and SEC22B.Cell discovery · 2023Article
- Dynamics of CLIMP-63 S-acylation control ER morphology.Nature communications · 2023Article
- Reconstitution of Fusion-Competent Human Placental Fusogen Syncytin-2.The Journal of membrane biology · 2022Article
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2 authors.
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Abstract
Membranes of the endoplasmic reticulum (ER) are shaped into cisternal sheets and cylindrical tubules. How ER sheets are generated and maintained is not clear. ER membrane protein Climp63 is enriched in sheets and routinely used as a marker of this structure. The luminal domain (LD) of Climp63 is predicted to be highly helical, and it may form bridges between parallel membranes, regulating the abundance and width of ER sheets. Here, we purified the LD and full-length (FL) Climp63 to analyze their homotypic interactions. The N-terminal tagged LD formed low-order oligomers in solution, but was extremely aggregation-prone when the GST tag was removed. Purified FL Climp63 formed detectable but moderate interactions with both the FL protein and the LD. When Climp63 was reconstituted into proteoliposomes with its LD facing out, the homotypic interactions were retained and could be competed by soluble LD, though vesicle clustering was not observed. These results demonstrate a direct self-association of Climp63, supporting its role as an ER luminal spacer.
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