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Nat Cell Biol. 2018 Mar;20(3):252-261. doi: 10.1038/s41556-017-0028-5. Epub 2018 Jan 29.

Local control of intracellular microtubule dynamics by EB1 photodissociation.

Author information

1
Department of Cell and Tissue Biology, University of California, San Francisco, CA, USA.
2
Institute of Epigenetics and Stem Cells, Helmholtz Center Munich, München, Germany.
3
University of North Carolina, Chapel Hill, NC, USA.
4
Department of Cell and Tissue Biology, University of California, San Francisco, CA, USA. torsten.wittmann@ucsf.edu.

Abstract

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 (π-EB1) by inserting a blue-light-sensitive protein-protein interaction module between the microtubule-binding and +TIP-binding domains of EB1. π-EB1 replaces endogenous EB1 function in the absence of blue light. By contrast, blue-light-mediated π-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 π-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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