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Structural basis for the self-recognition of sDSCAM in Chelicerata
Jie Cheng1, Yamei Yu2, Xingyu Wang2
1National Clinical Research Center for Geriatrics, West China Hospital, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, Sichuan University, 610041, Chengdu, China.
Nature Communications
|May 2, 2023
Summary
Shortened Dscam (sDscam) mediates cell recognition through a molecular zipper model. This study reveals sDscam
Area of Science:
- Neuroscience
- Molecular Biology
- Evolutionary Biology
Background:
- Neurons require molecular identity for neural circuit formation.
- Dscam and Pcdh families are crucial for synaptic specificity.
- Shortened Dscam (sDscam) in Chelicerata bridges Dscam and Pcdh functions.
Purpose of the Study:
- To elucidate the molecular mechanisms of sDscam self-recognition.
- To investigate both trans and cis interactions of sDscam.
- To propose a model for sDscam-mediated cell-cell recognition.
Main Methods:
- X-ray crystallography to determine sDscam structure.
- Functional assays to validate molecular interactions.
- Biophysical analyses of sDscam assembly.
Main Results:
- sDscam utilizes FNIII domains for cis interactions (side-by-side).
- sDscam employs Ig1 domains for trans interactions (hand-in-hand).
- A molecular zipper model explains sDscam assembly and recognition.
Conclusions:
- sDscam assembly is crucial for cell-cell recognition.
- The findings provide insights into the evolution of cell recognition molecules.
- This study offers a framework for understanding sDscam function and evolution.
