Structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (TOG) domain arrays

XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins....

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Vydáno v:	eLife Ročník 7
Hlavní autoři:	Nithianantham, Stanley, Cook, Brian D, Beans, Madeleine, Guo, Fei, Chang, Fred, Al-Bassam, Jawdat
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	England eLife Science Publications, Ltd 13.11.2018 eLife Sciences Publications Ltd eLife Sciences Publications, Ltd
Témata:	Alp14 Animation Biochemistry Cell adhesion & migration Cell Biology Crystallography, X-Ray Electron microscopy Fungal Proteins - chemistry Fungal Proteins - metabolism Fungi - metabolism Interfaces Mass spectrometry Microscopy Microscopy, Electron microtubule Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - metabolism Microtubules - chemistry Microtubules - metabolism Models, Molecular Money Peptides Polymer crosslinking Polymerization Protein Binding Protein Conformation Protein Multimerization Proteins Scientific imaging Structural Biology and Molecular Biophysics TOG domain Tubulin Tubulin - chemistry Tubulin - metabolism Tumors x-ray XMAP215 United States > US California XMAP215 microtubule cell biology x-ray S. pombe tubulin structural biology molecular biophysics Alp14 TOG domain
ISSN:	2050-084X, 2050-084X
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Abstract	XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins. Alp14 binds four tubulins via dimeric TOG1-TOG2 subunits, in which each domain exhibits a distinct exchange rate for tubulin. X-ray structures revealed square-shaped assemblies composed of pseudo-dimeric TOG1-TOG2 subunits assembled head-to-tail, positioning four unpolymerized tubulins in a polarized wheel-like configuration. Crosslinking and electron microscopy show Alp14-tubulin forms square assemblies in solution, and inactivating their interfaces destabilize this organization without influencing tubulin binding. An X-ray structure determined using approach to modulate tubulin polymerization revealed an unfurled assembly, in which TOG1-TOG2 uniquely bind to two polymerized tubulins. Our findings suggest a new microtubule polymerase model in which TOG arrays recruit tubulins by forming square assemblies that then unfurl, facilitating their concerted polymerization into protofilaments.
AbstractList	XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins. Alp14 binds four tubulins via dimeric TOG1-TOG2 subunits, in which each domain exhibits a distinct exchange rate for tubulin. X-ray structures revealed square-shaped assemblies composed of pseudo-dimeric TOG1-TOG2 subunits assembled head-to-tail, positioning four unpolymerized tubulins in a polarized wheel-like configuration. Crosslinking and electron microscopy show Alp14-tubulin forms square assemblies in solution, and inactivating their interfaces destabilize this organization without influencing tubulin binding. An X-ray structure determined using approach to modulate tubulin polymerization revealed an unfurled assembly, in which TOG1-TOG2 uniquely bind to two polymerized tubulins. Our findings suggest a new microtubule polymerase model in which TOG arrays recruit tubulins by forming square assemblies that then unfurl, facilitating their concerted polymerization into protofilaments. XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins. Alp14 binds four tubulins via dimeric TOG1-TOG2 subunits, in which each domain exhibits a distinct exchange rate for tubulin. X-ray structures revealed square-shaped assemblies composed of pseudo-dimeric TOG1-TOG2 subunits assembled head-to-tail, positioning four unpolymerized tubulins in a polarized wheel-like configuration. Crosslinking and electron microscopy show Alp14-tubulin forms square assemblies in solution, and inactivating their interfaces destabilize this organization without influencing tubulin binding. An X-ray structure determined using approach to modulate tubulin polymerization revealed an unfurled assembly, in which TOG1-TOG2 uniquely bind to two polymerized tubulins. Our findings suggest a new microtubule polymerase model in which TOG arrays recruit tubulins by forming square assemblies that then unfurl, facilitating their concerted polymerization into protofilaments.XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins. Alp14 binds four tubulins via dimeric TOG1-TOG2 subunits, in which each domain exhibits a distinct exchange rate for tubulin. X-ray structures revealed square-shaped assemblies composed of pseudo-dimeric TOG1-TOG2 subunits assembled head-to-tail, positioning four unpolymerized tubulins in a polarized wheel-like configuration. Crosslinking and electron microscopy show Alp14-tubulin forms square assemblies in solution, and inactivating their interfaces destabilize this organization without influencing tubulin binding. An X-ray structure determined using approach to modulate tubulin polymerization revealed an unfurled assembly, in which TOG1-TOG2 uniquely bind to two polymerized tubulins. Our findings suggest a new microtubule polymerase model in which TOG arrays recruit tubulins by forming square assemblies that then unfurl, facilitating their concerted polymerization into protofilaments.
Audience	Academic
Author	Nithianantham, Stanley Cook, Brian D Al-Bassam, Jawdat Beans, Madeleine Guo, Fei Chang, Fred
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Keywords	XMAP215 microtubule cell biology x-ray S. pombe tubulin structural biology molecular biophysics Alp14 TOG domain
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SubjectTerms	Alp14 Animation Biochemistry Cell adhesion & migration Cell Biology Crystallography, X-Ray Electron microscopy Fungal Proteins - chemistry Fungal Proteins - metabolism Fungi - metabolism Interfaces Mass spectrometry Microscopy Microscopy, Electron microtubule Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - metabolism Microtubules - chemistry Microtubules - metabolism Models, Molecular Money Peptides Polymer crosslinking Polymerization Protein Binding Protein Conformation Protein Multimerization Proteins Scientific imaging Structural Biology and Molecular Biophysics TOG domain Tubulin Tubulin - chemistry Tubulin - metabolism Tumors x-ray XMAP215
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