Coordinated Arp2/3-mediated actin branching and myosin-dependent force generation in membrane–cytoskeleton remodeling

The Arp2/3 (Actin-Related Protein 2/3) complex nucleates branched actin networks, while myosin motors generate force and reorganize actin through ATP-dependent motor activity. Their coordination is central to membrane remodeling, but the underlying mechanisms differ substantially among cellular processes and organisms. In this review, we distinguish direct molecular coupling from indirect mechanical coupling and signaling cross-talk. We also separate mechanisms established in fungal systems from those supported in mammalian cells. Across endocytosis, migration, secretion, membrane repair, and membrane fusion, Arp2/3 primarily determines where and how branched networks are nucleated, whereas polymerizing actin filaments generate protrusive or invaginating force. Distinct myosin isoforms then contribute membrane anchoring, contractile tension, network remodeling, or cargo transport. We further discuss membrane and cortical tension, retrograde flow, actin turnover, mTOR and Rho signaling, disease relevance, and unresolved questions. This mechanistic framework clarifies which aspects of Arp2/3–myosin coordination are experimentally demonstrated and which remain context-dependent models.

Authors

Institutions

Publication Details

Journal
Frontiers in Physiology
Published
2026-09-14
DOI
https://doi.org/10.3389/fphys.2026.1919458
Primary Topic
Cellular Mechanics and Interactions
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
article

Coordinated Arp2/3-mediated actin branching and myosin-dependent force generation in membrane–cytoskeleton remodeling

Chun‐Yi Jiang, Yifan Li, Jianghong He
Frontiers in Physiology
Cellular Mechanics and Interactions
article

Coordinated Arp2/3-mediated actin branching and myosin-dependent force generation in membrane–cytoskeleton remodeling

Chun‐Yi Jiang, Yifan Li, Jianghong He
article en

Abstract

The Arp2/3 (Actin-Related Protein 2/3) complex nucleates branched actin networks, while myosin motors generate force and reorganize actin through ATP-dependent motor activity. Their coordination is central to membrane remodeling, but the underlying mechanisms differ substantially among cellular processes and organisms. In this review, we distinguish direct molecular coupling from indirect mechanical coupling and signaling cross-talk. We also separate mechanisms established in fungal systems from those supported in mammalian cells. Across endocytosis, migration, secretion, membrane repair, and membrane fusion, Arp2/3 primarily determines where and how branched networks are nucleated, whereas polymerizing actin filaments generate protrusive or invaginating force. Distinct myosin isoforms then contribute membrane anchoring, contractile tension, network remodeling, or cargo transport. We further discuss membrane and cortical tension, retrograde flow, actin turnover, mTOR and Rho signaling, disease relevance, and unresolved questions. This mechanistic framework clarifies which aspects of Arp2/3–myosin coordination are experimentally demonstrated and which remain context-dependent models.

Frontiers in PhysiologyVol. 17
Anhui Medical University (CN), Nantong University (CN), Fuyang Second People's Hospital (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 15%
Cellular Mechanics and Interactions
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Coordinated Arp2/3-mediated actin branching and myosin-dependent force generation in membrane–cytoskeleton remodeling — Chun‐Yi Jiang, Yifan Li, et al. · Frontiers in Physiology (2026) | TGRS Research Map | TGRS