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ID 114343
タイトル別表記
The distinct distribution of two Dictyostelium Talins
著者
Tsujioka, Masatsune RIKEN Center for Developmental Biology|Tokyo Medical and Dental University
Uyeda, Taro Q. P. Waseda University
Iwadate, Yoshiaki Yamaguchi University
Patel, Hitesh The University of Edinburgh
柴田, 桂太朗 National Institute of Advanced Industrial Science and Technology (AIST)|National Institute of Information and Communications Technology 徳島大学 教育研究者総覧
Yumoto, Tenji Waseda University
米村, 重信 RIKEN Center for Developmental Biology|Tokushima University|RIKEN Center for Biosystems Dynamics Research 徳島大学 教育研究者総覧 KAKEN研究者をさがす
資料タイプ
学術雑誌論文
抄録
Although the distinct distribution of certain molecules along the anterior or posterior edge is essential for directed cell migration, the mechanisms to maintain asymmetric protein localization have not yet been fully elucidated. Here, we studied a mechanism for the distinct localizations of two Dictyostelium talin homologues, talin A and talin B, both of which play important roles in cell migration and adhesion. Using GFP fusion, we found that talin B, as well as its C-terminal actin-binding region, which consists of an I/LWEQ domain and a villin headpiece domain, was restricted to the leading edge of migrating cells. This is in sharp contrast to talin A and its C-terminal actin-binding domain, which co-localized with myosin II along the cell posterior cortex, as reported previously. Intriguingly, even in myosin II-null cells, talin A and its actin-binding domain displayed a specific distribution, co-localizing with stretched actin filaments. In contrast, talin B was excluded from regions rich in stretched actin filaments, although a certain amount of its actin-binding region alone was present in those areas. When cells were sucked by a micro-pipette, talin B was not detected in the retracting aspirated lobe where acto-myosin, talin A, and the actin-binding regions of talin A and talin B accumulated. Based on these results, we suggest that talin A predominantly interacts with actin filaments stretched by myosin II through its C-terminal actin-binding region, while the actin-binding region of talin B does not make such distinctions. Furthermore, talin B appears to have an additional, unidentified mechanism that excludes it from the region rich in stretched actin filaments. We propose that these actin-binding properties play important roles in the anterior and posterior enrichment of talin B and talin A, respectively, during directed cell migration.
掲載誌名
PLOS ONE
ISSN
19326203
出版者
PLOS
14
4
開始ページ
e0214736
発行日
2019-04-04
権利情報
© 2019 Tsujioka et al. This is an open access article distributed under the terms of the Creative Commons Attribution License( https://creativecommons.org/licenses/by/4.0/ ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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言語
eng
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部局
医学系