Literature DB >> 27432899

Correction: Talin tension sensor reveals novel features of focal adhesion force transmission and mechanosensitivity.

Abhishek Kumar, Mingxing Ouyang, Koen Van den Dries, Ewan James McGhee, Keiichiro Tanaka, Marie D Anderson, Alexander Groisman, Benjamin T Goult, Kurt I Anderson, Martin A Schwartz.   

Abstract

Entities:  

Year:  2016        PMID: 27432899      PMCID: PMC4949446          DOI: 10.1083/jcb.20151001207062016c

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


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Vol. 213 No. 3, May 9, 2016. Pages 371–383. In the original version of this article, the Discussion included the following text: While this manuscript was in revision, Austen et al. (2015) described an alternative talin-TS based on folded peptide hairpins that denature at forces in the 7–11-pN range. Although most of their results are consistent with ours, they found that a significant fraction of their 11-pN sensor was open in FAs, suggesting higher force. The hairpin, however, as expected for a folded domain, showed hysteresis when stretched in vitro; thus, it requires relatively high force to open but then can be maintained in the open state under lower tension. This sensor thus will report values that are biased toward the maximal forces, whereas the flagelliform spring is reversible and so should report mean tension. Analysis of forces on immobilized RGD peptides using folded domains or DNA hairpins also support the idea that peak forces can be high (Wang and Ha, 2013; Zhang et al., 2014; Galior et al., 2016), but these results cannot be interpreted as mean forces. After publication, the authors realized that the characterization of this related work was inaccurate. The new text reads: While this manuscript was in revision, Austen et al. (2015) described an alternative talin-TS based on folded peptide hairpins that denature at forces in the 7–11-pN range. Most of their results are consistent with ours; however, they found that a significant fraction of their 11-pN sensor was open in FAs, suggesting higher force. Any differences in reported tension across talin could be caused by some combination of differences in the way the in vitro calibrations are extrapolated to in vivo measurements or to differences in cell types and conditions. As a result of these changes, the references Wang and Ha, 2013; Zhang et al., 2014; and Galior et al., 2016 have been removed from the reference list. The authors apologize for any confusion this may have caused. The changes have been made in both the PDF and the online version. The error remains only in the print version.
  5 in total

1.  Mechanotransduction in talin through the interaction of the R8 domain with DLC1.

Authors:  Alexander William M Haining; Rolle Rahikainen; Ernesto Cortes; Dariusz Lachowski; Alistair Rice; Magdalena von Essen; Vesa P Hytönen; Armando Del Río Hernández
Journal:  PLoS Biol       Date:  2018-07-20       Impact factor: 8.029

Review 2.  Costameres, dense plaques and podosomes: the cell matrix adhesions in cardiovascular mechanosensing.

Authors:  Brian Sit; Daniel Gutmann; Thomas Iskratsch
Journal:  J Muscle Res Cell Motil       Date:  2019-06-18       Impact factor: 2.698

3.  Filamin A mediates isotropic distribution of applied force across the actin network.

Authors:  Abhishek Kumar; Maria S Shutova; Keiichiro Tanaka; Daniel V Iwamoto; David A Calderwood; Tatyana M Svitkina; Martin A Schwartz
Journal:  J Cell Biol       Date:  2019-07-17       Impact factor: 10.539

Review 4.  β2 Integrin Signaling Cascade in Neutrophils: More Than a Single Function.

Authors:  Panagiota Bouti; Steven D S Webbers; Susanna C Fagerholm; Ronen Alon; Markus Moser; Hanke L Matlung; Taco W Kuijpers
Journal:  Front Immunol       Date:  2021-02-18       Impact factor: 7.561

Review 5.  Biophysics of Cell-Substrate Interactions Under Shear.

Authors:  Neha Paddillaya; Ashish Mishra; Paturu Kondaiah; Pramod Pullarkat; Gautam I Menon; Namrata Gundiah
Journal:  Front Cell Dev Biol       Date:  2019-11-08
  5 in total

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