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Local control of intracellular microtubule dynamics by EB1 photodissociation.
Nat. Cell Biol. 20, 252–261 (2018)
End-binding proteins (EBs) are adaptors that recruit functionally diverse microtubule plus-end-tracking proteins (+TIPs) to growing microtubule plus ends. To test with high spatial and temporal accuracy how, when and where + TIP complexes contribute to dynamic cell biology, we developed a photo-inactivated EB1 variant (pi-EB1) by inserting a blue-light-sensitive protein-protein interaction module between the microtubule-binding and + TIP-binding domains of EB1 pi-EB1 replaces endogenous EB1 function in the absence of blue light. By contrast, blue-light-mediated pi-EB1 photodissociation results in rapid + TIP complex disassembly, and acutely and reversibly attenuates microtubule growth independent of microtubule end association of the microtubule polymerase CKAP5 (also known as ch-TOG and XMAP215). Local pi-EB1 photodissociation allows subcellular control of microtubule dynamics at the second and micrometre scale, and elicits aversive turning of migrating cancer cells. Importantly, light-mediated domain splitting can serve as a template to optically control other intracellular protein activities.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Plus End-tracking; Particle Tracking; Cell Motility; Living Cells; In-vitro; Proteins; Growth; Light; Reconstitution; Localization
ISSN (print) / ISBN
1465-7392
e-ISSN
1476-4679
Journal
Nature Cell Biology
Quellenangaben
Volume: 20,
Issue: 3,
Pages: 252–261
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Epigenetics and Stem Cells (IES)