Details

Autor(en) / Beteiligte

• Duan, Rui
• Kim, Ji Hoon
• Shilagardi, Khurts
• Schiffhauer, Eric S
• Lee, Donghoon M
• Son, Sungmin
• Li, Shuo
• Thomas, Claire
• Luo, Tianzhi
• Fletcher, Daniel A
• Robinson, Douglas N
• Chen, Elizabeth H

Titel

Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion

Ist Teil von

• Nature cell biology, 2018-06, Vol.20 (6), p.688

Ort / Verlag

England

Erscheinungsjahr

2018

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Spectrin is a membrane skeletal protein best known for its structural role in maintaining cell shape and protecting cells from mechanical damage. Here, we report that α/β -spectrin (β is also called karst) dynamically accumulates and dissolves at the fusogenic synapse between fusing Drosophila muscle cells, where an attacking fusion partner invades its receiving partner with actin-propelled protrusions to promote cell fusion. Using genetics, cell biology, biophysics and mathematical modelling, we demonstrate that spectrin exhibits a mechanosensitive accumulation in response to shear deformation, which is highly elevated at the fusogenic synapse. The transiently accumulated spectrin network functions as a cellular fence to restrict the diffusion of cell-adhesion molecules and a cellular sieve to constrict the invasive protrusions, thereby increasing the mechanical tension of the fusogenic synapse to promote cell membrane fusion. Our study reveals a function of spectrin as a mechanoresponsive protein and has general implications for understanding spectrin function in dynamic cellular processes.