Please use this identifier to cite or link to this item:
|Title:||Differential mechanical stability of filamin A rod segments|
|Authors:||Chen, H. |
|Citation:||Chen, H., Zhu, X., Cong, P., Sheetz, M.P., Nakamura, F., Yan, J. (2011-09-07). Differential mechanical stability of filamin A rod segments. Biophysical Journal 101 (5) : 1231-1237. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bpj.2011.07.028|
|Abstract:||Prompted by recent reports suggesting that interaction of filamin A (FLNa) with its binding partners is regulated by mechanical force, we examined mechanical properties of FLNa domains using magnetic tweezers. FLNa, an actin cross-linking protein, consists of two subunits that dimerize through a C-terminal self-association domain. Each subunit contains an N-terminal spectrin-related actin-binding domain followed by 24 immunoglobulinlike (Ig) repeats. The Ig repeats in the rod 1 segment (repeats 1-15) are arranged as a linear array, whereas rod 2 (repeats 16-23) is more compact due to interdomain interactions. In the rod 1 segment, repeats 9-15 augment F-actin binding to a much greater extent than do repeats 1-8. Here, we report that the three segments are unfolded at different forces under the same loading rate. Remarkably, we found that repeats 16-23 are susceptible to forces of ∼10 pN or even less, whereas the repeats in the rod 1 segment can withstand significantly higher forces. The differential force response of FLNa Ig domains has broad implications, since these domains not only support the tension of actin network but also interact with many transmembrane and signaling proteins, mostly in the rod 2 segment. In particular, our finding of unfolding of repeats 16-23 at ∼10 pN or less is consistent with the hypothesized force-sensing function of the rod 2 segment in FLNa. © 2011 Biophysical Society.|
|Source Title:||Biophysical Journal|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Nov 10, 2018
WEB OF SCIENCETM
checked on Oct 16, 2018
checked on Sep 29, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.