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First published online 3 November 2009
doi: 10.1242/jcs.048439

Journal of Cell Science 122, 4319-4329 (2009)
Published by The Company of Biologists 2009
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Research Article

Localization of nectin-free afadin at the leading edge and its involvement in directional cell movement induced by platelet-derived growth factor

Muneaki Miyata1, Hisakazu Ogita1, Hitomi Komura1, Shinsuke Nakata2, Ryoko Okamoto2, Misa Ozaki1, Takashi Majima2, Naomi Matsuzawa1, Satoshi Kawano1, Akihiro Minami1, Masumi Waseda1, Naoyuki Fujita2, Kiyohito Mizutani1, Yoshiyuki Rikitake1 and Yoshimi Takai1,*

1 Division of Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan
2 Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine, Osaka 565-0871 Japan

* Author for correspondence (ytakai{at}med.kobe-u.ac.jp)

Accepted 21 September 2009

Afadin is an actin-filament-binding protein that binds to nectin, an immunoglobulin-like cell-cell adhesion molecule, and plays an important role in the formation of adherens junctions. Here, we show that afadin, which did not bind to nectin and was localized at the leading edge of moving cells, has another role: enhancement of the directional, but not random, cell movement. When NIH3T3 cells were stimulated with platelet-derived growth factor (PDGF), afadin colocalized with PDGF receptor, {alpha}vβ3 integrin and nectin-like molecule-5 at the leading edge and facilitated the formation of leading-edge structures and directional cell movement in the direction of PDGF stimulation. However, these phenotypes were markedly perturbed by knockdown of afadin, and were dependent on the binding of afadin to active Rap1. Binding of Rap1 to afadin was necessary for the recruitment of afadin and the tyrosine phosphatase SHP-2 to the leading edge. SHP-2 was previously reported to tightly regulate the activation of PDGF receptor and its downstream signaling pathway for the formation of the leading edge. These results indicate that afadin has a novel role in PDGF-induced directional cell movement, presumably in cooperation with active Rap1 and SHP-2.

Key words: Growth factor receptor, Integrin, Nectin-like molecule, SHP-2


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© The Company of Biologists Ltd 2009