Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bpj.2011.07.028
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dc.titleDifferential mechanical stability of filamin A rod segments
dc.contributor.authorChen, H.
dc.contributor.authorZhu, X.
dc.contributor.authorCong, P.
dc.contributor.authorSheetz, M.P.
dc.contributor.authorNakamura, F.
dc.contributor.authorYan, J.
dc.date.accessioned2014-05-19T02:51:17Z
dc.date.available2014-05-19T02:51:17Z
dc.date.issued2011-09-07
dc.identifier.citationChen, 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
dc.identifier.issn00063495
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/52876
dc.description.abstractPrompted 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bpj.2011.07.028
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentPHYSICS
dc.description.doi10.1016/j.bpj.2011.07.028
dc.description.sourcetitleBiophysical Journal
dc.description.volume101
dc.description.issue5
dc.description.page1231-1237
dc.description.codenBIOJA
dc.identifier.isiut000294653800025
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