Identification of ?III- and ?IV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): Antibody mapping and cDNA sequencing

Modig, Carina; Olsson, Per‐Erik; Barasoaín, Isabel; Inés, Concepción de; Andreu, José Manuel; Roach, Mary Carmen; Ludueña, Richard F.; Wallin, Margareta

doi:10.1002/(sici)1097-0169(1999)42:4<315::aid-cm5>3.0.co;2-c

Cited by 14 publications

(10 citation statements)

References 55 publications

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“…The IgG fraction of a nonimmune rabbit serum was purified as described previously (34) and concentrated as the other IgGs. P11E12 (anti-␤-tubulin N-terminal) and P12E11 (anti-␣-tubulin C-terminal) mouse monoclonal IgGs were obtained as described previously (35)(36)(37). MOPC 21-purified mouse IgG was from Sigma.…”

Section: Methodsmentioning

confidence: 99%

Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface

Díaz

Barasoaín

Souto

et al. 2005

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface

Díaz

Barasoaín

Souto

et al. 2005

Journal of Biological Chemistry

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“…Class I (Constitutive; Human h␤1) ␤I EEEEDFGEEAEEEA Class II ('Major brain' or 'major neuronal') ␤II DEQGEFEEEEGEDEA Class III ('Minor brain' or 'minor neuronal'; Human h␤4) ␤III EEEGEMYEDDDEESEAQGPK Class IVa ('Brain specific'; Human ␤5) ␤IVa EEGEFEEEAEEEVA Class IVb ('Major testis'; Human h␤2) ␤IVb EEEGEFEEEAEEEVA Class V ('Avian specific'; Chick c␤5) ␤V NDGEEAFEDEDEEEEINE Class VI ('Hematopoietic') ␤VI GLEDSEEDAEEAEVEAEDKDII al., 1982;Dietrich et al, 1987;Burgoyne et al, 1988;Caccamo et al, 1989a;Moody et al, 1989;Lee et al, 1990a,b;Easter et al, 1993;Katsetos et al, 1993;Ludueña, 1998;Farina et al, 1999;Modig et al, 1999]. However, ␤III protein is not detectable in the developing or mature Xenopus nervous system.…”

Section: Table I ␤-Tubulin Isotypesmentioning

confidence: 99%

Class III β‐tubulin in human development and cancer

Katsetos

Herman²,

Mörk

2003

Cell Motil. Cytoskeleton

262

188

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The differential cellular expression of class III ␤-tubulin isotype (␤III) is reviewed in the context of human embryological development and neoplasia. As compared to somatic organs and tissues, ␤III is abundant in the central and peripheral nervous systems (CNS and PNS) where it is prominently expressed during fetal and postnatal development. As exemplified in cerebellar and sympathoadrenal neurogenesis, the distribution of ␤III is neuron-associated, exhibiting distinct temporospatial gradients according to the regional neuroepithelia of origin. However, transient expression of this protein is also present in the subventricular zones of the CNS comprising putative neuronal-and/or glial precursor cells, as well as in Kulchitsky neuroendocrine cells of the fetal respiratory epithelium. This temporally restricted, potentially non-neuronal expression may have implications in the identification of presumptive neurons derived from embryonic stem cells. In adult tissues, the distribution of ␤III is almost exclusively neuron-specific. Altered patterns of expression are noted in cancer. In "embryonal"-and "adult-type" neuronal tumors of the CNS and PNS, ␤III is associated with neuronal differen- Abbreviations: bHLH, basic helix-loop-helix; ␤III, class III ␤-tubulin isotype, CNE , central nervous system enhancer; CNS, central nervous system; EGL, external granule layer; MAP, microtubule-associated protein; NCAM, neural cell adhesion molecule; OPC, oligodendrocyte precursor cell; PCNA, proliferating cell nuclear antigen; PNS, peripheral nervous system; pRb, retinoblastoma tumor suppressor protein; PSA, polysialated; SVZ, subventricular zone; WHO, World Health Organization. tiation and decreased cell proliferation. In contrast, the presence of ␤III in gliomas and lung cancer is associated with an ascending histological grade of malignancy. Thus, ␤III expression in neuronal tumors is differentiation-dependent, while in non-neuronal tumors it is aberrant and/or represents "dedifferentiation" associated with the acquisition of progenitor-like phenotypic properties. Increased expression in various epithelial cancer cell lines is associated with chemoresistance to taxanes. Because ␤III is present in subpopulations of neoplastic, but not in normal differentiated glial or somatic epithelial cells, the elucidation of mechanisms responsible for the altered expression of this isotype may provide insights into the role of the microtubule cytoskeleton in tumorigenesis and tumor progression. Cell Motil. Cytoskeleton 55: 77-96, 2003.

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“…Thus, the interspecific conservation of ␤-chain isotypes that typifies higher vertebrates appears not to hold for the more distantly related fishes. Three brain ␤-tubulin sequences (␤1-␤3; GenBank TM accession numbers AF102890, AAD56401, and AF184595, respectively) from the Atlantic cod (Gadus morhua), a northern marine fish that typically lives at 8 -15°C but is able to acclimatize to near-freezing temperatures in winter, have been described (24). Although the southern notothenioids and northern gadoids diverged long before their respective oceans cooled (25,26), some of the unique ␤-chain substitutions of the Antarctic fishes were present in one or more of the gadid chains (e.g.…”

Section: Fig 2 Frequency Histograms Of Rates Of Microtubule Growth mentioning

confidence: 99%

Cold Adaptation of Microtubule Assembly and Dynamics

Detrich¹,

Parker²,

Williams³

et al. 2000

Journal of Biological Chemistry

143

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The microtubules of Antarctic fishes, unlike those of homeotherms, assemble at very low temperatures (؊1.8°C). The adaptations that enhance assembly of these microtubules are intrinsic to the tubulin dimer and reduce its critical concentration for polymerization at 0°C to ϳ0.9 mg/ml (Williams, R. C., Jr., Correia, J. J., and DeVries, A. L. (1985) Biochemistry 24, 2790 -2798). Here we demonstrate that microtubules formed by pure brain tubulins of Antarctic fishes exhibit slow dynamics at both low (5°C) and high (25°C) temperatures; the rates of polymer growth and shortening and the frequencies of interconversion between these states are small relative to those observed for mammalian microtubules (37°C). To investigate the contribution of tubulin primary sequence variation to the functional properties of the microtubules of Antarctic fishes, we have sequenced brain cDNAs that encode 9 ␣-tubulins and 4 ␤-tubulins from the yellowbelly rockcod Notothenia coriiceps and 4 ␣-tubulins and 2 ␤-tubulins from the ocellated icefish Chionodraco rastrospinosus. The tubulins of these fishes were found to contain small sets of unique or rare residue substitutions that mapped to the lateral, interprotofilament surfaces or to the interiors of the ␣-and ␤-polypeptides; longitudinal interaction surfaces are not altered in the fish tubulins. Four changes (A278T and S287T in ␣; S280G and A285S in ␤) were present in the S7-H9 interprotofilament "M" loops of some monomers and would be expected to increase the flexibility of these regions. A fifth lateral substitution specific to the ␣-chain (M302L or M302F) may increase the hydrophobicity of the interprotofilament interaction. Two hydrophobic substitutions (␣:S187A in helix H5 and ␤:Y202F in sheet S6) may act to stabilize the monomers in conformations favorable to polymerization. We propose that cold adaptation of microtubule assembly in Antarctic fishes has occurred in part by evolutionary restructuring of the lateral surfaces and the cores of the tubulin monomers.The capacity of the cytoplasmic tubulins of Antarctic fishes to form microtubules at temperatures as low as Ϫ1.8°C, the freezing point of the seawater habitat of these fish, is remarkable. The critical concentration for polymerization at 0°C of purified, MAP 1 -free brain tubulin is ϳ0.9 mg/ml (1-3), which approximates the values observed for mammalian brain tubulins at 37°C (1, 4). Unlike mammalian microtubules, however, the cytoplasmic microtubules of Antarctic fishes are very stable and exhibit slow dynamics at cold temperatures (5, 6). Evidently, both the capacity to polymerize at low critical concentration and the slow exchange of tubulin dimers into and out of microtubule polymers are properties intrinsic to the tubulin subunits of these fishes. These unusual functional characteristics must be explicable by structural alterations to the primary sequences and/or by changes in the posttranslational modifications of the tubulin chains that, alone or in concert, modify the quaternary interactions between dimers in a microtu...

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Identification of ?III- and ?IV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): Antibody mapping and cDNA sequencing

Cited by 14 publications

References 55 publications

Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface

Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface

Class III β‐tubulin in human development and cancer

Cold Adaptation of Microtubule Assembly and Dynamics

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