A protein, Tetrahymena p85, is localized to the presumptive division plane before the formation of the contractile ring. p85 directly interacts with Tetrahymena calmodulin (CaM) in a Ca2+-dependent manner, and p85 and CaM colocalize in the division furrow. A Ca2+/CaM inhibitor N-(6- Aminohexyl)-5-chloro-1-naphthalenesulfonamide HCl (W7) inhibits the direct interaction between p85 and Ca2+/CaM. W7 also inhibits the localization of p85 and CaM to the division plane, and the formation of the contractile ring and division furrow. Tetrahymena fimbrin and elongation factor-1a (EF-1α), which induce bundling of Tetrahymena F-actin, are also localized to the division furrow during cytokinesis. The Tetrahymena fimbrin has two actin- binding domains, but lacks the EF-hand Ca2+-binding motif, suggesting that Tetrahymena fimbrin probably crosslinks actin filaments in a Ca2+- insensitive manner during cytokinesis. The evidence also indicates that Ca2+/CaM inhibits the F-actin-bundling activity of EF-1α; and EF-1α and CaM colocalize in the division furrow. In this review, we propose that the Ca2+/CaM signal and its target protein p85 cooperatively regulate the determination of the division plane, and that a Ca2+-insensitive actin- bundling protein, Tetrahymena fimbrin, and a Ca2+/CaM-sensitive actin- bundling protein, EF-1α, play pivotal roles in regulating the organization of the contractile ring microfilaments. (C) 2000 Wiley-Liss, Inc.
|Number of pages||9|
|Journal||Microscopy Research and Technique|
|Publication status||Published - 2000 Apr 15|
ASJC Scopus subject areas
- Medical Laboratory Technology