ADF/cofilin is not essential but is critically important for actin activities during phagocytosis in Tetrahymena thermophila

Nanami Shiozaki, Kentaro Nakano*, Yasuharu Kushida, Taro Q.P. Noguchi, Taro Q.P. Uyeda, Dorota Wloga, Drashti Dave, Krishna Kumar Vasudevan, Jacek Gaertig, Osamu Numataa

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

ADF/cofilin is a highly conserved actin-modulating protein. Reorganization of the actin cytoskeleton in vivo through severing and depolymerizing of F-actin by this protein is essential for various cellular events, such as endocytosis, phagocytosis, cytokinesis, and cell migration. We show that in the ciliate Tetrahymena thermophila, the ADF/cofilin homologue Adf73p associates with actin on nascent food vacuoles. Overexpression of Adf73p disrupted the proper localization of actin and inhibited the formation of food vacuoles. In vitro, recombinant Adf73p promoted the depolymerization of filaments made of T. thermophila actin (Act1p). Knockout cells lacking the ADF73 gene are viable but grow extremely slowly and have a severely decreased rate of food vacuole formation. Knockout cells have abnormal aggregates of actin in the cytoplasm. Surprisingly, unlike the case in animals and yeasts, in Tetrahymena, ADF/cofilin is not required for cytokinesis. Thus, the Tetrahymena model shows promise for future studies of the role of ADF/cofilin in vivo.

Original languageEnglish
Pages (from-to)1080-1086
Number of pages7
JournalEukaryotic Cell
Volume12
Issue number8
DOIs
Publication statusPublished - 2013 Aug
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'ADF/cofilin is not essential but is critically important for actin activities during phagocytosis in Tetrahymena thermophila'. Together they form a unique fingerprint.

Cite this