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Eukaryotic Cell, May 2008, p. 906-916, Vol. 7, No. 5
1535-9778/08/$08.00+0     doi:10.1128/EC.00464-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Overlapping Functions of the Two Talin Homologues in Dictyostelium ^,

Masatsune Tsujioka,^1,2* Kunito Yoshida,^3, Akira Nagasaki,¹ Shigenobu Yonemura,² Annette Müller-Taubenberger,⁴ and Taro Q. P. Uyeda¹

National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan,¹ RIKEN, Center for Developmental Biology, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan,² Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan,³ Institute for Cell Biology (ABI), Ludwig Maximilians University, Schillerstr. 42, 80336 Munich, Germany⁴

Received 27 December 2007/ Accepted 18 March 2008

Talin is a cytoskeletal protein involved in constructing and regulating focal adhesions in animal cells. The cellular slime mold Dictyostelium discoideum has two talin homologues, talA and talB, and earlier studies have characterized the single knockout mutants. talA^– cells show reduced adhesion to the substrates and slightly impaired cytokinesis leading to a high proportion of multinucleated cells in the vegetative stage, while the development is normal. In contrast, talB^– cells are characterized by reduced motility in the developmental stage, and they are arrested at the tight-mound stage. Here, we created and analyzed a double mutant with a disruption of both talA and talB. Defects in adhesion to the substrates, cytokinesis, and development were more severe in cells with a disruption of both talA and talB. The talA^– talB^– cells failed to attach to the substrates in the vegetative stage, exhibited a higher proportion of multinucleated cells than talA^– cells, and showed more-reduced motility during the development and an earlier developmental arrest than talB^– cells at the loose-mound stage. Moreover, overexpression of either talA or talB compensated for the loss of the other talin, respectively. The analysis of talA^– talB^– cells also revealed that talin was required for the formation of paxillin-rich adhesion sites and that there was another adhesion mechanism which is independent of talin in the developmental stage. This is the first study demonstrating overlapping functions of two talin homologues, and our data further indicate the importance of talin.

Published ahead of print on 28 March 2008.

Supplemental material for this article may be found at http://ec.asm.org/.

Present address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom.