Polymerization and Calcium Binding of the Tubulin-colchicine Complex in the GDP State

Doi, Hiroshi; Kawaguchi, Makiko; Timasheff, Serge N.

doi:10.1271/bbb.67.1643

Cited by 4 publications

(1 citation statement)

References 42 publications

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“…Another reason may be the contribution of calpain, which is regulated by calcium, to AD. Instead of tubulin, the tubulin-colchicine complex was used (Doi, H., et al, 2003a). The high affinity sites of calcium took part in the polymerization of the complex in the GTP state, while the low ones participated in the depolymerization.…”

Section: Polymerization and Calcium Binding To Tubulin-colchicine Commentioning

confidence: 99%

Roles of Microtubules in Maintenance of Nerve Cell Networks

Yomogida¹,

Yoshida-Yamamoto²,

Doi³

2011

Neurodegenerative Diseases - Processes, Prevention, Protection and Monitoring

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Section: Polymerization and Calcium Binding To Tubulin-colchicine Commentioning

confidence: 99%

Roles of Microtubules in Maintenance of Nerve Cell Networks

Yomogida¹,

Yoshida-Yamamoto²,

Doi³

2011

Neurodegenerative Diseases - Processes, Prevention, Protection and Monitoring

Self Cite

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Membranous and structural damage that occur during cryopreservation of human sperm may be time-related events

Desrosiers

Légaré

Leclerc

et al. 2006

Fertility and Sterility

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The C Terminus of Tubulin, a Versatile Partner for Cationic Molecules

Lefèvre¹,

Chernov

Joshi

et al. 2011

Journal of Biological Chemistry

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The C-terminal region of tubulin is involved in multiple aspects of the regulation of microtubule assembly. To elucidate the molecular mechanisms of this regulation, we study here, using different approaches, the interaction of Tau Microtubules are involved in a number of critical cellular processes, such as the determination of cell shape, chromosome segregation, intracellular transport of vesicles and organelles, and cell migration. Microtubules consist mainly of ␣␤-tubulin heterodimers organized head-to-tail into protofilaments whose parallel self-association gives rise to microtubules (1-4). ␣-and ␤-tubulin monomers have each a molecular mass of 50 kDa and are organized in three domains, namely the N-terminal domain (amino acid residues 1-205) involved in nucleotide binding, the intermediate domain (amino acid residues 206 -384), and the C-terminal domain (amino acid residue 385 to the C terminus) (5). The C-terminal domain of tubulin represents a critical part of the binding site of different tubulin/microtubules partners, such as MAPs, 4 which are major regulators of microtubule dynamics (6 -8), or polycations, which promote tubulin assembly in vitro in different polymeric forms (9). The C-terminal domain comprises a highly negatively charged tail of about 20 amino acid residues (named herein the C-terminal tail (CTT)), which protrudes from the surface of microtubules. In agreement with its participation in the regulation of microtubule assembly through interactions with partners, the CTT is also the most divergent part of tubulin, and variations among tubulin isotypes (10) may explain the modulation of the dynamics of microtubule assembly in specific tissues or cytoplasmic regions.Different structure information has been obtained regarding the C-terminal domain of tubulin by using either fulllength tubulin or peptide fragments. Electron crystallography of zinc-induced tubulin sheets showed the presence of two anti-parallel ␣-helices (helix H11 (amino acid residues 385-397) and helix H12 (amino acid residues 418 -433)) lying at the outer surface of tubulin. The regions corresponding to the CTTs of either ␣-or ␤-tubulin were however not observed, probably due to the flexibility of this part of the protein (5). These observations were confirmed by x-ray diffraction analyses of crystal complexes formed between tubulin and the RB3-stathmin-like domain (11-13). Other structural data were obtained with peptides from the C-terminal region of tubulin studied either when free in solution or in interaction with different partners. NMR structure investigations on ␣-and ␤-tubulin C-terminal peptides showed that both ␣ (residues 404 -451) and ␤ (residues 394 -445) peptides have no defined secondary structure in aqueous solution but contain a well □ S The on-line version of this article (available at http://www.jbc.org) contains supplemental 4 The abbreviations used are: MAP, microtubule-associated protein; ␣Tub410C, amino acid residues 410 -451 from ␣1a-tubulin; CTT, tubulin C-terminal tail; ITC, isothermal titration ...

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Polymerization and Calcium Binding of the Tubulin-colchicine Complex in the GDP State

Cited by 4 publications

References 42 publications

Roles of Microtubules in Maintenance of Nerve Cell Networks

Roles of Microtubules in Maintenance of Nerve Cell Networks

Membranous and structural damage that occur during cryopreservation of human sperm may be time-related events

The C Terminus of Tubulin, a Versatile Partner for Cationic Molecules

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