Kyoko Okada's research while affiliated with Brandeis University and other places
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Publications (5)
The tumor suppressor protein adenomatous polyposis coli (APC) regulates cell protrusion and cell migration, processes that require the coordinated regulation of actin and microtubule dynamics. APC localizes in vivo to microtubule plus ends and actin-rich cortical protrusions, and has well-documented direct effects on microtubule dynamics. However,...
Adenomatous polyposis coli (APC) protein has emerged as a complex, multifunctional regulator in the Wnt-signaling pathway and in controlling the actin and microtubule cytoskeleton during basic cellular events such as cell polarization, migration, adhesion, chromosome segregation, and apoptosis. Here we demonstrate that APC directly binds F-actin an...
Adenomatous polyposis coli (APC) protein is a large tumor suppressor that is truncated in most colorectal cancers. The carboxyl-terminal
third of APC protein mediates direct interactions with microtubules and the microtubule plus-end tracking protein EB1. In
addition, APC has been localized to actin-rich regions of cells, but the mechanism and func...
Rapid turnover of actin structures is required for dynamic remodeling of the cytoskeleton and cell morphogenesis, but the mechanisms driving actin disassembly are poorly defined. Cofilin plays a central role in promoting actin turnover by severing/depolymerizing filaments. Here, we analyze the in vivo function of a ubiquitous actin-interacting prot...
Working in concert, multiple actin-binding proteins regulate the dynamic turnover of actin networks. Here, we define a novel function for the conserved actin-binding protein twinfilin, which until now was thought to function primarily as a monomer-sequestering protein. We show that purified budding yeast twinfilin (Twf1) binds to and severs actin f...
Citations
... Significant advancements have been made in understanding the interactions between actin and microtubules through in vitro reconstitution (Griffith and Pollard, 1978) and cell-free reconstitution (Sider et al., 1999;Waterman-Storer et al., 2000;Colin et al., 2018) over the past four decades. These reconstitution approaches have been proven valuable in understanding the effects of proteins operating at the interface between actin and microtubule on nucleation (Okada et al., 2010;Henty-Ridilla et al., 2016), stability (Bartolini et al., 2008) and coorganization of these filaments (Sattilaro, 1986;Roger et al., 2004;Preciado López et al., 2014;Elie et al., 2015). Yet, elucidating the cooperative behavior and mutual influence of cytoskeletal components in living cells still present considerable challenges. ...
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... Twinfilin 1 (TWF1) as an inhibitor of the actin polymerization is involved in regulation of cell migration, drug sensitivity, and tumor progression [152,153]. Inhibition of the SBF2-AS1 decreased the levels of TWF1 expressions via miR-142-3p sponging to increase GEM resistance in pancreatic tumor cells [154]. EMT is one of the pathophysiological cellular processes that is involved in regulation of embryogenesis, tumor metastasis, and drug resistance [155]. ...
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... Abp140, which bundles F-actin, decorates both patches and cables (Asakura et al., 1998;Yang and Pon, 2002). Cables and patches both appear to be disassembled by cofilin, Aip1, and Srv2/CAP (Lappalainen et al., 1997;Rodal et al., 1999;Okada et al., 2006;Drubin, 2007, 2010;Chaudhry et al., 2013;Ydenberg et al., 2015;Pollard et al., 2020). While cofilin, Aip1, and Srv2/CAP are clearly visible on patches by immunofluorescence and GFP-tagging, these proteins are not readily detected on cables. ...
... The cytoskeleton interacts with various signaling molecules, including the well-known tumor suppressor adenomatous polyposis coli (APC), to influence cellular functions. APC associates with actin and microtubule through the basic domain and interacts with β-catenin together with the tumor suppressor Axin and the Ser/Thr kinases glycogen synthase kinase-3 (GSK-3) in the destruction complex within the cytoplasm [21,22]. The dissociation of β-catenin from APC facilitates its nuclear translocation to activate Wnt/β-catenin signaling, which is critical in the maintenance of self-renewal. ...
