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Nat Cell Biol. 2018 Jun;20(6):688-698. doi: 10.1038/s41556-018-0106-3. Epub 2018 May 25.

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

Author information

1
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
2
Laboratory of Regenerative Medicine in Sports Science, School of Sports Science, South China Normal University, Guangzhou, China.
3
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
4
Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX, USA.
5
Department of Bioengineering, University of California, Berkeley, Berkeley, CA, USA.
6
Departments of Biology and of Biochemistry and Molecular Biology, Penn State University, University Park, PA, USA.
7
Department of Modern Mechanics, University of Science and Technology of China, Hefei, China.
8
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA. Elizabeth.Chen@UTSouthwestern.edu.
9
Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX, USA. Elizabeth.Chen@UTSouthwestern.edu.

Abstract

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/βH-spectrinH 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.

PMID:
29802406
DOI:
10.1038/s41556-018-0106-3

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