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TitleMechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins.
Journal, issue, pagesCell, Vol. 162, Issue 4, Page 849-859, Year 2015
Publish dateAug 13, 2015
AuthorsRui Zhang / Gregory M Alushin / Alan Brown / Eva Nogales /
PubMed AbstractMicrotubule (MT) dynamic instability is driven by GTP hydrolysis and regulated by microtubule-associated proteins, including the plus-end tracking end-binding protein (EB) family. We report six cryo- ...Microtubule (MT) dynamic instability is driven by GTP hydrolysis and regulated by microtubule-associated proteins, including the plus-end tracking end-binding protein (EB) family. We report six cryo-electron microscopy (cryo-EM) structures of MTs, at 3.5 Å or better resolution, bound to GMPCPP, GTPγS, or GDP, either decorated with kinesin motor domain after polymerization or copolymerized with EB3. Subtle changes around the E-site nucleotide during hydrolysis trigger conformational changes in α-tubulin around an "anchor point," leading to global lattice rearrangements and strain generation. Unlike the extended lattice of the GMPCPP-MT, the EB3-bound GTPγS-MT has a compacted lattice that differs in lattice twist from that of the also compacted GDP-MT. These results and the observation that EB3 promotes rapid hydrolysis of GMPCPP suggest that EB proteins modulate structural transitions at growing MT ends by recognizing and promoting an intermediate state generated during GTP hydrolysis. Our findings explain both EBs end-tracking behavior and their effect on microtubule dynamics.
External linksCell / PubMed:26234155 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution3.3 - 4.4 Å
Structure data

EMDB-6347:
Cryo-EM structure of GTPgammaS microtubule co-polymerized with EB3
Method: EM (helical sym.) / Resolution: 3.4 Å

EMDB-6348:
Cryo-EM structure of GTPgammaS-microtubule co-polymerized with EB3 and decorated with kinesin
Method: EM (helical sym.) / Resolution: 3.5 Å

6349

3jak

EMDB-6349, PDB-3jak:
Cryo-EM structure of GTPgammaS-microtubule co-polymerized with EB3 (merged dataset with and without kinesin bound)
Method: EM (helical sym.) / Resolution: 3.3 Å

6350

3jal

EMDB-6350, PDB-3jal:
Cryo-EM structure of GMPCPP-microtubule co-polymerized with EB3
Method: EM (helical sym.) / Resolution: 3.5 Å

6351

3jar

EMDB-6351, PDB-3jar:
Cryo-EM structure of GDP-microtubule co-polymerized with EB3
Method: EM (helical sym.) / Resolution: 3.4 Å

6352

3jat

EMDB-6352, PDB-3jat:
Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin
Method: EM (helical sym.) / Resolution: 3.5 Å

6353

3jas

EMDB-6353, PDB-3jas:
Cryo-EM structure of dynamic GDP-microtubule (14 protofilaments) decorated with kinesin
Method: EM (helical sym.) / Resolution: 3.5 Å

6354

3jaw

EMDB-6354: Asymmetric (C1) reconstruction of EB3-bound microtubule (merged dataset containing tubulin bound to GTPgammaS, GMPCPP and GDP)
PDB-3jaw: Atomic model of a microtubule seam based on a cryo-EM reconstruction of the EB3-bound microtubule (merged dataset containing tubulin bound to GTPgammaS, GMPCPP, and GDP)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-6355:
Asymmetric (C1) reconstruction of GMPCPP-microtubule (13 protofilaments) decorated with kinesin
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-GSP:
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE

ChemComp-G2P:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogue*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

Source
  • sus scrofa (pig)
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / microtubule / EB3 / GTPgammaS / kinesin / GMPCPP / GDP / seam

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