Actin cytoskeleton disruption shortens worm lifespan, while mild stabilization extends it
On August 24, a bibliographic record of an iScience article appeared in Crossref. In the full text, authors altered actin cytoskeleton function in the roundworm Caenorhabditis elegans: network disruption shortened life, while mild chemical stabilization extended it; a high dose produced the opposite effect.
The actin cytoskeleton helps muscles contract, maintains intestinal cell junctions, and participates in intracellular transport. In prior work from the same research line, increased production of the BET‑1 protein preserved actin in old worms and extended their lifespan.
The new study examines the converse: what happens when the network loses order. Authors sequentially weakened actin and three proteins that direct its assembly, disassembly, and anchoring. In muscle, intestine, and cuticle, filaments lost normal organization earlier, and mobility declined with age. In some worms, gene activity resembled that of older animals.
Because the age of intervention matters — in another C. elegans experiment, transient NuA4 suppression in early development extended lifespan, while later intervention shortened it — part of the new experiments began on the first day of adult life. Lifespan reduction persisted upon suppression of arx-2, a component of the Arp2/3 complex that builds branched actin networks.
Separately, adult worms were given two substances. Latrunculin A breaks actin filaments and, with increasing dose, shortened life. Jasplakinolide helps filaments assemble and stabilize: at low concentrations it extended life, at high concentrations it shortened. Authors link the harm of high doses to overly stabilized filaments being less able to remodel.
Actin disruption simultaneously altered mitochondrial shape and function, protein homeostasis, cellular component recycling, and intestinal barrier integrity. In two independent human cohorts, authors also correlated ACTB gene variants with the pace of age‑related walking slowdown.
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iScience
Form and function of actin impacts actin health and aging
Cell biology; Bioinformatics; Omics
