7MFW

Drosophila melanogaster Canoe PDZ domain in complex with Echinoid C-terminal region

7MFW の概要

• エントリーDOI: 10.2210/pdb7mfw/pdb
• 分子名称: Canoe,Echinoid (2 entities in total)
• 機能のキーワード: afadin, canoe, pdz, echinoid, cell adhesion
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21761.09

構造登録者

Slep, K.C.,Peifer, M.,Byrnes, A.E. (登録日: 2021-04-11, 公開日: 2021-11-10, 最終更新日: 2023-10-18)

主引用文献

Perez-Vale, K.Z.,Yow, K.D.,Johnson, R.I.,Byrnes, A.E.,Finegan, T.M.,Slep, K.C.,Peifer, M.
Multivalent interactions make adherens junction-cytoskeletal linkage robust during morphogenesis.
J.Cell Biol., 220:-, 2021

PubMed Abstract: Embryogenesis requires cells to change shape and move without disrupting epithelial integrity. This requires robust, responsive linkage between adherens junctions and the actomyosin cytoskeleton. Using Drosophila morphogenesis, we define molecular mechanisms mediating junction-cytoskeletal linkage and explore the role of mechanosensing. We focus on the junction-cytoskeletal linker Canoe, a multidomain protein. We engineered the canoe locus to define how its domains mediate its mechanism of action. To our surprise, the PDZ and FAB domains, which we thought connected junctions and F-actin, are not required for viability or mechanosensitive recruitment to junctions under tension. The FAB domain stabilizes junctions experiencing elevated force, but in its absence, most cells recover, suggesting redundant interactions. In contrast, the Rap1-binding RA domains are critical for all Cno functions and enrichment at junctions under tension. This supports a model in which junctional robustness derives from a large protein network assembled via multivalent interactions, with proteins at network nodes and some node connections more critical than others.

PubMed: 34762121
DOI: 10.1083/jcb.202104087

実験手法

X-RAY DIFFRACTION (2.104 Å)