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TitleTubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics.
Journal, issue, pagesElife, Vol. 4, Year 2015
Publish dateJul 24, 2015
AuthorsStanley Nithianantham / Sinh Le / Elbert Seto / Weitao Jia / Julie Leary / Kevin D Corbett / Jeffrey K Moore / Jawdat Al-Bassam /
PubMed AbstractMicrotubule dynamics and polarity stem from the polymerization of αβ-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate α- and β-tubulin assembly into ...Microtubule dynamics and polarity stem from the polymerization of αβ-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate α- and β-tubulin assembly into heterodimers and maintain the soluble tubulin pool in the cytoplasm, but their physical mechanisms are unknown. Here, we reconstitute a core tubulin chaperone consisting of tubulin cofactors TBCD, TBCE, and Arl2, and reveal a cage-like structure for regulating αβ-tubulin. Biochemical assays and electron microscopy structures of multiple intermediates show the sequential binding of αβ-tubulin dimer followed by tubulin cofactor TBCC onto this chaperone, forming a ternary complex in which Arl2 GTP hydrolysis is activated to alter αβ-tubulin conformation. A GTP-state locked Arl2 mutant inhibits ternary complex dissociation in vitro and causes severe defects in microtubule dynamics in vivo. Our studies suggest a revised paradigm for tubulin cofactors and Arl2 functions as a catalytic chaperone that regulates soluble αβ-tubulin assembly and maintenance to support microtubule dynamics.
External linksElife / PubMed:26208336 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 24.0 Å
Structure data

EMDB-6390:
Tubulin cofactors-D,E and Arl2-Q73L GTPase form a stable heterotrimeric chaperone
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-6391:
Tubulin cofactors-D,E(N-GFP) and Arl2-Q73L GTPase form a stable heterotrimeric chaperone
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-6392:
Structural basis for TBC-DEG assembly with soluble tubulin dimer
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-6393:
Structural basis for TBC-DEG assembly with TBCC and soluble tubulin dimer
Method: EM (single particle) / Resolution: 24.0 Å

PDB-5cya:
Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-HOH:
WATER / Water

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • unidentified (others)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsCHAPERONE / Tubulin cofactors / mirotubule dynamics / tubulin chaperones / Arl2 GTPase-activating protein TBCC / GAP activity / beta helix / beta-sheets

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