The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex

Gigant, B.; Curmi, Patrick A.; Martin-Barbey, Carole; Charbaut, Elodie; Lachkar, Sylvie; Lebeau, Luc; Siavoshian, S; Sobel, André; Knossow, M.

doi:10.1016/s0092-8674(00)00069-6

Cited by 248 publications

(277 citation statements)

References 41 publications

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“…This is likely mediated predominantly by stress-activated JNK signaling as JNK inhibition substantially reduces OS-induced phosphorylation at that site (14). The STMN Ser-38 residue is located in a disordered linker region that does not interact with tubulin (39), and prior in vitro studies have suggested that Ser-38 phosphorylation had marginal effects in on STMN-tubulin binding and microtubule-destabilizing activity (11,28), which were confirmed by our current investigations (Fig. 9H).…”

Section: Discussionsupporting

confidence: 91%

cAMP-dependent Protein Kinase and c-Jun N-terminal Kinase Mediate Stathmin Phosphorylation for the Maintenance of Interphase Microtubules during Osmotic Stress

Yip

Yeap

Bogoyevitch

et al. 2014

Journal of Biological Chemistry

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Background: Complex phosphorylation mechanisms negatively regulate stathmin microtubule-destabilizing activity. Results: Stathmin is co-regulated by JNK and PKA to maintain the integrity of interphase microtubules during hyperosmotic stress. Conclusion: Stress-activated JNK and PKA pathways are integrated in the regulation of the microtubule array during cell stress. Significance: Stress signaling regulation of microtubule destabilizing stathmin is critical in determining cytoskeleton organization in response to cell stress.

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Section: Discussionsupporting

confidence: 91%

cAMP-dependent Protein Kinase and c-Jun N-terminal Kinase Mediate Stathmin Phosphorylation for the Maintenance of Interphase Microtubules during Osmotic Stress

Yip

Yeap

Bogoyevitch

et al. 2014

Journal of Biological Chemistry

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“…of C␣ positions: 0.8 Å, within the range expected for identical structures, given the resolution of the corresponding diffraction data]. Therefore, the main function of the RB3-SLD C-terminal helix is to hold tubulin heterodimers together in T 2 R in relative orientations that are consistent with low resolution images of curved tubulin assemblies that do not comprise RB3-SLD and are obtained with or without colchicine (20). We summarize here the movements within subunits that give rise to the subunits orientation changes on going from a curved to a straight assembly.…”

Section: Discussionsupporting

confidence: 53%

“…2 A). The RB3-SLD C-terminal helix only contacts residues in the nucleotide binding domain and in the C-terminal helical hairpin (20), an ensemble that is unchanged in T 2 R with respect to straight protofilaments [root mean square deviation (r.m.s.d.) of C␣ positions: 0.8 Å, within the range expected for identical structures, given the resolution of the corresponding diffraction data].…”

Section: Discussionmentioning

confidence: 99%

Variations in the colchicine-binding domain provide insight into the structural switch of tubulin

Dorléans

Gigant

Ravelli

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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285

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Structural changes occur in the ␣␤-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to a curved structure. There is a broad range of small molecule compounds that disturbs the microtubule cycle, a class of which targets the colchicine-binding site and prevents microtubule assembly. This class includes compounds with very different chemical structures, and it is presently unknown whether they prevent tubulin polymerization by the same mechanism. To address this issue, we have determined the structures of tubulin complexed with a set of such ligands and show that they interfere with several of the movements of tubulin subunits structural elements upon its transition from curved to straight. We also determined the structure of tubulin unliganded at the colchicine site; this reveals that a ␤-tubulin loop (termed T7) flips into this site. As with colchicine site ligands, this prevents a helix which is at the interface with ␣-tubulin from stacking onto a ␤-tubulin ␤ sheet as in straight protofilaments. Whereas in the presence of these ligands the interference with microtubule assembly gets frozen, by flipping in and out the ␤-subunit T7 loop participates in a reversible way in the resistance to straightening that opposes microtubule assembly. Our results suggest that it thereby contributes to microtubule dynamic instability.cytoskeleton ͉ inhibitors ͉ microtubules

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“…5). Although SulA has no sequence homologues in eukaryotes, a similar mechanism is seen with the tubulin-binding protein stathmin, which sequesters tubulin dimers, although it disrupts lateral interactions between protofilaments rather than acting via the T7 loop to affect interactions within the protofilament (35). The second effect of SulA is binding to preformed FtsZ filaments.…”

Section: Resultsmentioning

confidence: 99%

Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ

Cordell

Robinson

Löwe

2003

Proc. Natl. Acad. Sci. U.S.A.

220

180

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SulA halts cell division in Escherichia coli by binding to the major component of the division machinery FtsZ. We have solved the crystal structure of SulA alone and in complex with FtsZ from Pseudomonas aeruginosa. SulA is expressed when the SOS response is induced. This is a mechanism to inhibit cell division and repair DNA in the event of DNA damage. FtsZ is a tubulin-like protein that forms polymers, with the active-site GTPase split across two monomers. One monomer provides the GTP-binding site and the other, through its T7 loop nucleotide hydrolysis. Our structures show that SulA is a dimer, and that SulA inhibits cell division neither by binding the nucleotide-binding site nor by inducing conformational changes in FtsZ. Instead, SulA binds the T7 loop surface of FtsZ, opposite the nucleotide-binding site, blocking polymer formation. These findings explain why GTP hydrolysis and polymer turnover are required for SulA inhibition.

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The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex

Cited by 248 publications

References 41 publications

cAMP-dependent Protein Kinase and c-Jun N-terminal Kinase Mediate Stathmin Phosphorylation for the Maintenance of Interphase Microtubules during Osmotic Stress

cAMP-dependent Protein Kinase and c-Jun N-terminal Kinase Mediate Stathmin Phosphorylation for the Maintenance of Interphase Microtubules during Osmotic Stress

Variations in the colchicine-binding domain provide insight into the structural switch of tubulin

Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ

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