Rapid signal transduction in living cells is a unique feature of mechanotransduction.

@article{citeulike:2763434, abstract = {It is widely postulated that mechanotransduction is initiated at the local force-membrane interface by inducing local conformational changes of proteins, similar to soluble ligand-induced signal transduction. However, all published reports are limited in time scale to address this fundamental issue. Using a FRET-based cytosolic Src reporter in a living cell, we quantified changes of Src activities as a local stress via activated integrins was applied. The stress induced rapid (<0.3 s) activation of Src at remote cytoplasmic sites, which depends on the cytoskeletal prestress. In contrast, there was no Src activation within 12 s of soluble epidermal growth factor (EGF) stimulation. A 1.8-Pa stress over a focal adhesion activated Src to the same extent as 0.4 ng/ml EGF at long times (minutes), and the energy levels for mechanical stimulation and chemical stimulation were comparable. The effect of both stress and EGF was less than additive. Nanometer-scale cytoskeletal deformation analyses revealed that the strong activation sites of Src by stress colocalized with large deformation sites of microtubules, suggesting that microtubules are essential structures for transmitting stresses to activate cytoplasmic proteins. These results demonstrate that rapid signal transduction via the prestressed cytoskeleton is a unique feature of mechanotransduction.}, address = {Departments of Mechanical Science and Engineering and.}, author = {Na, Sungsoo and Collin, Olivier and Chowdhury, Farhan and Tay, Bernard and Ouyang, Mingxing and Wang, Yingxiao and Wang, Ning }, citeulike-article-id = {2763434}, doi = {http://dx.doi.org/10.1073/pnas.0711704105}, issn = {1091-6490}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {cell-adhesion, mechanotransduction}, month = {May}, posted-at = {2008-05-07 02:53:12}, priority = {3}, title = {Rapid signal transduction in living cells is a unique feature of mechanotransduction.}, url = {http://dx.doi.org/10.1073/pnas.0711704105}, year = {2008} }

TY - JOUR ID - citeulike:2763434 L3 - citeulike-article-id:2763434 TI - Rapid signal transduction in living cells is a unique feature of mechanotransduction. JF - Proceedings of the National Academy of Sciences of the United States of America AD - Departments of Mechanical Science and Engineering and. SN - 1091-6490 N2 - It is widely postulated that mechanotransduction is initiated at the local force-membrane interface by inducing local conformational changes of proteins, similar to soluble ligand-induced signal transduction. However, all published reports are limited in time scale to address this fundamental issue. Using a FRET-based cytosolic Src reporter in a living cell, we quantified changes of Src activities as a local stress via activated integrins was applied. The stress induced rapid (<0.3 s) activation of Src at remote cytoplasmic sites, which depends on the cytoskeletal prestress. In contrast, there was no Src activation within 12 s of soluble epidermal growth factor (EGF) stimulation. A 1.8-Pa stress over a focal adhesion activated Src to the same extent as 0.4 ng/ml EGF at long times (minutes), and the energy levels for mechanical stimulation and chemical stimulation were comparable. The effect of both stress and EGF was less than additive. Nanometer-scale cytoskeletal deformation analyses revealed that the strong activation sites of Src by stress colocalized with large deformation sites of microtubules, suggesting that microtubules are essential structures for transmitting stresses to activate cytoplasmic proteins. These results demonstrate that rapid signal transduction via the prestressed cytoskeleton is a unique feature of mechanotransduction. KW - cell-adhesion KW - mechanotransduction AU - Na, Sungsoo AU - Collin, Olivier AU - Chowdhury, Farhan AU - Tay, Bernard AU - Ouyang, Mingxing AU - Wang, Yingxiao AU - Wang, Ning PY - 2008/05/02/ UR - http://dx.doi.org/10.1073/pnas.0711704105 ER -