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Watari, S.

Publications and source records attributed to Watari, S..

2 recordsLinked to original sources

A genetically encoded microtubule bundler for causal dissection of microtubule bundling in cells

Microtubule (MT) bundling is a conserved organizational feature of the cytoskeleton that accompanies MT stabilization, suggesting that it is involved in diverse cellular processes, including mitosis, migration, and axon morphogenesis. Although microtubule-associated proteins are known to induce MT bundling, whether bundling itself is sufficient to alter MT properties and cellular behavior has remained difficult to address due to the lack of tools that selectively manipulate MT bundling in living cells. Here, we describe the development of a genetically encoded, protein-based "MT-Bundler" by coupling an MT-binding motif to a biologically inert oligomerization scaffold, enabling direct and tunable crosslinking of intracellular MTs. The expression of MT-Bundler consisting of MAP4 and Azami-Green, drove robust MT bundling, but also conferred marked resistance to depolymerization, and elevated MT acetylation. Functionally, enforced MT bundling disrupts cell division and migration and suppresses neurite and axon outgrowth. To confirm the causal relationship behind these findings, we further engineered chemically and optically inducible MT-Bundlers that permit rapid, reversible, and spatiotemporally precise control of MT bundling. Acute induction of MT bundling triggers a rapid increase in MT acetylation, revealing bundling as an upstream organizational cue that promotes luminal access of the acetyltransferase ATAT1. Notably, MT stabilization persists even in the absence of acetylation, demonstrating that bundling itself is sufficient to mechanically stabilize MTs. Together, these results identify MT bundling as a primary determinant of MT stability and modification, establishing MT-Bundlers as a versatile tool to dissect the mechanistic basis of MT bundling in living cells.

bioengineering↗

Optical Control of Microtubule Accumulation and Dispersion by Tau-Derived Peptide-Fused Photo-Responsive Protein

Microtubules, a major component of the cytoskeleton consisting of tubulin dimers, are involved in various cellular functions, including forming axons and dendrites of neurons and retaining cell shapes by forming various accumulated superstructures such as bundles and doublets. Moreover, microtubule-accumulated structures like swarming microtubule assemblies are attractive components for dynamic materials, such as active matter and molecular robots. Thus, dynamic control of microtubule superstructures is an important topic. However, implementing stimulus-dependent control of superstructures remains challenging. This challenge can be resolved by developing designer protein approaches. We have previously developed a Tau-derived peptide (TP), which binds to the inner or outer surface of microtubules depending on the timing of the incubation. In this report, we designed the TP-fused photo-switchable protein Dronpa (TP-Dronpa) that reversibly photoconverts between monomeric and tetrameric states to photocontrol microtubule assemblies. The formation of microtubule superstructures, including bundles and doublets, was induced by tetrameric TP-Dronpa, whereas monomeric TP-Dronpa ensured that microtubules remained dispersed. Tetrameric TP-Dronpa also induced motile aster-like structures and swarming movement of microtubules on a kinesin-coated substrate. The formation/dissociation of these microtubule superstructures can be controlled by light irradiation. This system can generate and photocontrol various microtubule superstructures and provides an approach to facilitate the assembly of dynamic materials for various applications. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=131 SRC="FIGDIR/small/614838v1_ufig1.gif" ALT="Figure 1"> View larger version (29K): org.highwire.dtl.DTLVardef@fdcc92org.highwire.dtl.DTLVardef@81bf32org.highwire.dtl.DTLVardef@2f7f5eorg.highwire.dtl.DTLVardef@52fc9f_HPS_FORMAT_FIGEXP M_FIG C_FIG

bioengineering↗