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Structures of TOG1 and TOG2 From the Human Microtubule Dynamics Regulator CLASP1

Jonathan B. Leano, View ORCID ProfileKevin C. Slep
doi: https://doi.org/10.1101/479766
Jonathan B. Leano
1Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, North Carolina, 27599, United States of America
2Program in Molecular and Cellular Biophysics, University of North Carolina, Chapel Hill, North Carolina, 27599, United States of America
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Kevin C. Slep
2Program in Molecular and Cellular Biophysics, University of North Carolina, Chapel Hill, North Carolina, 27599, United States of America
3Department of Biology, University of North Carolina, Campus Box 3280, Chapel Hill, North Carolina, 27599, United States of America
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Abstract

Tubulin-binding TOG domains are found arrayed in a number of proteins that regulate microtubule dynamics. While much is known about the structure and function of TOG domains in the XMAP215 microtubule polymerase family, less in known about the TOG domain array found in the CLASP family. The CLASP TOG array promotes microtubule pause, potentiates rescue, and limits catastrophe. How distinct the TOG domains of CLASP are from one another, from XMAP215 TOG domains, and whether they are positionally conserved across CLASP family members is poorly understood. We present the x-ray crystal structures of human CLASP1 TOG1 and TOG2. The structures of CLASP1 TOG1 and TOG2 are distinct from each other, from CLASP TOG3, and are positionally conserved across species. While studies have failed to detect CLASP TOG1 tubulin-binding activity, TOG1 is structurally similar to the free-tubulin binding TOG domains of XMAP215. In contrast, though CLASP TOG2 and TOG3 have tubulin binding activity, they are structurally distinct from the free-tubulin binding TOG domains of XMAP215. CLASP TOG2 has a convex architecture, predicted to engage a hyper-curved tubulin state. CLASP TOG3 has unique structural elements in the C-terminal half of its α-solenoid domain that modeling studies implicate in binding to laterally-associated tubulin subunits in the microtubule lattice in a mode similar to, yet distinct from XMAP215 TOG4. These findings highlight the structural diversity of TOG domains within the CLASP TOG array and provide a molecular foundation for understanding CLASP-dependent effects on microtubule dynamics.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted November 26, 2018.
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Structures of TOG1 and TOG2 From the Human Microtubule Dynamics Regulator CLASP1
Jonathan B. Leano, Kevin C. Slep
bioRxiv 479766; doi: https://doi.org/10.1101/479766
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Structures of TOG1 and TOG2 From the Human Microtubule Dynamics Regulator CLASP1
Jonathan B. Leano, Kevin C. Slep
bioRxiv 479766; doi: https://doi.org/10.1101/479766

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