論文

査読有り
2017年

Nano-mechanical characterization of tension-sensitive helix bundles in talin rod

Biochemical and Biophysical Research Communications
  • Maki, K.
  • ,
  • Nakao, N.
  • ,
  • Adachi, T.

484
2
開始ページ
372
終了ページ
377
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbrc.2017.01.127
出版者・発行元
ACADEMIC PRESS INC ELSEVIER SCIENCE

Tension-induced exposure of a cryptic signaling binding site is one of the most fundamental mechanisms in molecular mechanotransduction. Helix bundles in rod domains of talin, a tension-sensing protein at focal adhesions, unfurl under tension to expose cryptic vinculin binding sites. Although the difference in their mechanical stabilities would determine which helix bundle is tension-sensitive, their respective mechanical behaviors under tension have not been characterized. In this study, we evaluated the mechanical behaviors of residues 486-654 and 754-889 of talin, which form helix bundles with low and high tension-sensitivity, by employing AFM nano-tensile testing. As a result, residues 754-889 exhibited lower unfolding energy for complete unfolding than residues 486-654. In addition, we found that residues 754-889 transition into intermediate conformations under lower tension than residues 486-654. Furthermore, residues 754-889 showed shorter persistence length in the intermediate conformation than residues 486-654, suggesting that residues 754-889 under tension exhibit separated alpha-helices, while residues 486-654 assume a compact conformation with inter-helix interactions. Therefore, we suggest that residues 754-889 of talin work as a tension-sensitive domain to recruit vinculin at the early stage of focal adhesion development, while residues 486-654 contribute to rather robust tension-sensitivity by recruiting vinculin under high tension. (C) 2017 Elsevier Inc. All rights reserved.

リンク情報
DOI
https://doi.org/10.1016/j.bbrc.2017.01.127
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000394735400024&DestApp=WOS_CPL
URL
http://www.scopus.com/inward/record.url?eid=2-s2.0-85011115829&partnerID=MN8TOARS
ID情報
  • DOI : 10.1016/j.bbrc.2017.01.127
  • ISSN : 0006-291X
  • eISSN : 1090-2104
  • ORCIDのPut Code : 38324046
  • SCOPUS ID : 85011115829
  • Web of Science ID : WOS:000394735400024

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