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Author Notes:

Correspondence to: Shoichiro Ono, Department of Pathology, Emory University, 615 Michael Street, Whitehead Research Building, Room 105N, Atlanta, GA 30322, Tel: (404) 727-3916, Fax: (404) 727-8538, sono@emory.edu


Research Funding:

National Institute of Arthritis and Musculoskeletal and Skin Diseases : NIAMS

This work was supported by a grant from the National Institute of Health (R01 AR48615) to S. O.


  • Actin filaments
  • nematode
  • myofibrils
  • stress
  • overexpression

Actin-ADF/cofilin rod formation in Caenorhabditis elegans muscle requires a putative F-actin binding site of ADF/cofilin at the C-terminus


Journal Title:

Cell Motility and the Cytoskeleton


Volume 66, Number 7


, Pages 398-408

Type of Work:

Article | Post-print: After Peer Review


Under a number of stress or pathological conditions, actin and actin depolymerizing factor (ADF)/cofilin form rod-like structures that contain abnormal bundles of actin filaments that are heavily decorated with ADF/cofilin. However, the mechanism of actin rod formation and the physiological role of actin rods are not clearly understood. Here, we report that overexpression of green fluorescent protein-fused UNC-60B, a muscle-specific ADF/cofilin isoform, in Caenorhabditis elegans body wall muscle induces formation of rod-like structures. The rods contained GFP-UNC-60B, actin-interacting protein 1 (AIP1), and actin, but not other major actin-associated proteins, thus resembling actin-ADF/cofilin rods found in other organisms. However, depletion or overexpression of AIP1 did not affect formation of the actin-GFP-UNC-60B rods, suggesting that AIP1 does not play a significant role in the rod assembly. Truncation of the C-terminal tail, a putative F-actin binding site, of UNC-60B abolished induction of the rod formation, strongly suggesting that stable association of UNC-60B with F-actin, which is mediated by its C-terminus, is required for inducing actin-ADF/cofilin rods. This study suggests that C. elegans can be a new model to study functions of actin-ADF/cofilin rods.

Copyright information:

© 2009 Wiley-Liss, Inc.

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