DAPLE orchestrates apical actomyosin assembly from junctional polarity complexes.
Arthur Marivin1, Rachel Xi-Yeen Ho1, Mikel Garcia-Marcos1
1Department of Biochemistry, Boston University School of Medicine, Boston, MA.
The PAR polarity complex recruits DAPLE to cell junctions, linking polarity to cytoskeletal organization. This mechanism ensures proper epithelial cell shape by stabilizing actin and activating RhoA-myosin signaling.
Area of Science:
- Cell Biology
- Epithelial Biology
- Cytoskeletal Dynamics
Background:
- Epithelial cells require coordinated polarity and cytoskeletal organization for proper function.
- The molecular mechanisms linking polarity complexes to cytoskeletal regulation of cell shape are not fully understood.
Purpose of the Study:
- To elucidate the mechanism by which the PAR polarity complex influences cytoskeletal organization at apical junctions.
- To identify the molecular players involved in translating polarity cues into cytoskeletal dynamics.
Main Methods:
- Investigated the role of the PAR polarity complex (PAR3-PAR6-aPKC) in epithelial cell morphology.
- Utilized techniques to identify proteins recruited by the PAR complex to apical junctions.
- Examined the downstream effects of recruited proteins on actin stabilization and RhoA-myosin signaling.
Main Results:
- The PAR polarity complex recruits DAPLE to apical cell junctions.
- DAPLE triggers a two-pronged mechanism for apical actomyosin assembly.
- DAPLE recruits CD2AP for actin stabilization and activates G protein signaling for RhoA-myosin activation.
Conclusions:
- DAPLE acts as a direct molecular link between junctional polarity complexes and apical cytoskeletal assemblies.
- This pathway is crucial for maintaining epithelial cell morphology.
- The findings reveal a novel mechanism for regulating cell shape through polarity-cytoskeleton crosstalk.
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