In situ structure of actin remodeling during glucose-stimulated insulin secretion using cryo-electron tomography

Weimin Li, Angdi Li, Bing Yu, Xiaoxiao Zhang, Xiaoyan Liu, Kate L. White, Raymond C. Stevens, Wolfgang Baumeister (), Andrej Sali (), Marion Jasnin () and Liping Sun ()
Additional contact information
Weimin Li: ShanghaiTech University
Angdi Li: ShanghaiTech University
Bing Yu: ShanghaiTech University
Xiaoxiao Zhang: ShanghaiTech University
Xiaoyan Liu: ShanghaiTech University
Kate L. White: University of Southern California
Raymond C. Stevens: ShanghaiTech University
Wolfgang Baumeister: ShanghaiTech University
Andrej Sali: University of California, San Francisco
Marion Jasnin: Helmholtz Pioneer Campus, Helmholtz Zentrum München
Liping Sun: ShanghaiTech University

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract Actin mediates insulin secretion in pancreatic β-cells through remodeling. Hampered by limited resolution, previous studies have offered an ambiguous depiction as depolymerization and repolymerization. We report the in situ structure of actin remodeling in INS-1E β-cells during glucose-stimulated insulin secretion at nanoscale resolution. After remodeling, the actin filament network at the cell periphery exhibits three marked differences: 12% of actin filaments reorient quasi-orthogonally to the ventral membrane; the filament network mainly remains as cell-stabilizing bundles but partially reconfigures into a less compact arrangement; actin filaments anchored to the ventral membrane reorganize from a “netlike” to a “blooming” architecture. Furthermore, the density of actin filaments and microtubules around insulin secretory granules decreases, while actin filaments and microtubules become more densely packed. The actin filament network after remodeling potentially precedes the transport and release of insulin secretory granules. These findings advance our understanding of actin remodeling and its role in glucose-stimulated insulin secretion.

Date: 2024
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DOI: 10.1038/s41467-024-45648-7

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