Imperial College London

DrArmandoDel Rio Hernandez

Faculty of EngineeringDepartment of Bioengineering

Senior Lecturer



+44 (0)20 7594 5187a.del-rio-hernandez




308Bessemer BuildingSouth Kensington Campus






BibTex format

author = {Haining, AWM and Rahikainen, R and Cortes, E and Lachowski, D and Rice, A and von, Essen M and Hytonen, VP and Hernandez, ADR},
doi = {10.1371/journal.pbio.2005599},
journal = {PLoS Biology},
title = {Mechanotransduction in talin through the interaction of the R8 domain with DLC1},
url = {},
volume = {16},
year = {2018}

RIS format (EndNote, RefMan)

AB - The mechanical unfolding of proteins is a cellular mechanism for force transduction with potentially broad implications in cell fate. Despite this, the mechanism by which protein unfolding elicits differential downstream signalling pathways remains poorly understood. Here, we used protein engineering, atomic force microscopy, and biophysical tools to delineate how protein unfolding controls cell mechanics. Deleted in liver cancer 1 (DLC1) is a negative regulator of Ras homolog family member A (RhoA) and cell contractility that regulates cell behaviour when localised to focal adhesions bound to folded talin. Using a talin mutant resistant to force-induced unfolding of R8 domain, we show that talin unfolding determines DLC1 downstream signalling and, consequently, cell mechanics. We propose that this new mechanism of mechanotransduction may have implications for a wide variety of associated cellular processes.
AU - Haining,AWM
AU - Rahikainen,R
AU - Cortes,E
AU - Lachowski,D
AU - Rice,A
AU - von,Essen M
AU - Hytonen,VP
AU - Hernandez,ADR
DO - 10.1371/journal.pbio.2005599
PY - 2018///
SN - 1544-9173
TI - Mechanotransduction in talin through the interaction of the R8 domain with DLC1
T2 - PLoS Biology
UR -
UR -
UR -
VL - 16
ER -