Regulation of tubulin synthesis during the cell cycle in the synchronous plasmodia of <i>Physarum polycephalum</i>

Ducommun, Bernard; Cance, J.; Wright, Michel

doi:10.1002/jcp.1041450117

Cited by 5 publications

(8 citation statements)

References 38 publications

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“…Once produced, tubulin proteins tend to be rather stable, with half-lives ranging between 15-50 hrs depending on the cellular model (Caron et al, 1985a;Mooney et al, 1994;Semotok and Lipshitz, 2007). However, this half-life is not absolute but subject to tissue type (Burow et al, 2015), culture substrate (Mooney et al, 1994) and cell-cycle state (Ducommun et al, 1990). Furthermore, tubulins can be recycled for new rounds of polymerisation (Nogales and Wang, 2006), as illustrated also by in vitro studies with purified brain tubulin which can be repeatedly polymerised and depolymerised (e.g.)…”

Section: Regulating Tubulin Availability In Axonsmentioning

confidence: 99%

A conceptual view at microtubule plus end dynamics in neuronal axons

Voelzmann

Hahn

Pearce

et al. 2016

Preprint

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Axons are the cable-like protrusions of neurons which wire up the nervous system. Polar bundles of microtubules (MTs) constitute their structural backbones and are highways for lifesustaining transport between proximal cell bodies and distal synapses. Any morphogenetic changes of axons during development, plastic rearrangement, regeneration or degeneration depend on dynamic changes of these MT bundles. A key mechanism for implementing such changes is the coordinated polymerisation and depolymerisation at the plus ends of MTs within these bundles. To gain an understanding of how such regulation can be achieved at the cellular level, we provide here an integrated overview of the extensive knowledge we have about the molecular mechanisms regulating MT de/polymerisation. We first summarise insights gained from work in vitro, then describe the machinery which supplies the essential tubulin building blocks, the protein complexes associating with MT plus ends, and MT shaft-based mechanisms that influence plus end dynamics. We briefly summarise the contribution of MT plus end dynamics to important cellular functions in axons, and conclude by discussing the challenges and potential strategies of integrating the existing molecular knowledge into conceptual understanding at the level of axons.

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Section: Regulating Tubulin Availability In Axonsmentioning

confidence: 99%

A conceptual view at microtubule plus end dynamics in neuronal axons

Voelzmann

Hahn

Pearce

et al. 2016

Preprint

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“…However, 3H-leucine incorporation data revealed that IC has minimal effect on the synthesis of vimentin and induces a slight decrease in the synthesis rate of a-actin and a-tubulin in OCLE cells. Vimentin synthesis is generally regulated by growth stimulators and thus it is not surprising to observe minimal or no effect of IC on vimentin synthesis by OCLE cells [Traub et al, 1983;Jarvinen, 1990;Tsuru et al, 19901. However, TCLE cells showed significant increase in the rate of a-tubulin synthesis in response to IC [Da Silva and Juliani, 1988;Ducomnun et al, 1990;Fernyhough and Ishii, 1987;Fernyhough et al, 1989;Wheatley et al, 19883. The a-actin and vimentin synthesis of TCLE cells was not significantly altered by IC.…”

Section: Discussionmentioning

confidence: 99%

The mammalian iris‐ciliary complex affects organization and synthesis of cytoskeletal protein of organ and tissue cultured lens epithelial cells

Banerjee¹,

Emanuel²,

Parafina³

et al. 1992

J of Cellular Biochemistry

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A water soluble growth inhibitor was isolated from the mammalian ocular iris-ciliary complex. The molecular weight of this protein is 10 kD or lower as determined by ultrafiltration fractionation. The iris-ciliary (IC) complex water soluble protein(s) significantly inhibits synthesis of lower molecular weight proteins of the epithelial cells of the organ cultured mammalian ocular lens. It was also found that this inhibitory effect of IC is mediated via the structural organization of the lens. Monolayer cultures of the lens epithelial cells exposed to IC did not manifest any inhibition of their protein synthesis. Moreover, these tissue cultured lens epithelial (TCLE) cells showed a significant increase in their protein synthetic activities in response to the presence of IC factors in the culture medium. It is postulated that the IC activity is modulated via either the lens capsule, an extracellular matrix, or due to the specific organization of the intact lens. The specific effects of IC on the cytoskeletal organization and synthesis in the organ cultured lens epithelial (OCLE) and TCLE cells were also examined. Both groups, treated with IC factors, manifested significant alterations in their protein synthetic activities and cytoskeletal architecture. The 3H-leucine incorporation experiments showed that alpha-actin and alpha-tubulin synthesis is partially inhibited by IC factors in OCLE cells but vimentin synthesis is not, whereas in TCLE cells all of them showed increased synthesis in response to IC factors. Turnover rates of these proteins in both OCLE and TCLE cells were also computed. The immunofluorescence and microscopic evaluation of OCLE and TCLE cells exposed to IC factors illustrated significant alteration in the cytoarchitecture of the filaments. We demonstrate that an inhibitor(s) molecule of 10 kD or lower size isolated from IC inhibited protein synthesis of OCLE cells and stimulated protein synthesis in TCLE cells. The IC factor also affects the synthesis and organization of cytoskeletal filaments of both the OCLE and TCLE cells.

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“…Physarum strains, culture and microscopy Plasmodia (strain CL) were cultured and prepared as described by Ducommun and Wright (1989). Synchronous giant plasmodia (approximately 10cm diameter), grown at 22°C except when stated otherwise, were used before or after the third synchronous mitosis.…”

Section: Methodsmentioning

confidence: 99%

“…This model offers a unique opportunity for following a biochemical event in a single cell during a normal cell cycle or after physical or pharmacological perturbations (Tyson, 1982). Previous studies using this organism have permitted the characterization of the pathways involved in the regulation of tubulin synthesis (Ducommun et al, unpublished data) and degradation (Ducommun and Wright, 1989), and the regulation of thymidine kinase synthesis (Wright and Tollon, 1979, 1989Eon-Gerhardt et al 1981a,6).…”

Section: Introductionmentioning

confidence: 99%

Cell cycle regulation of p34 cdc2 kinase activity in Physarum polycephalum

Ducommun

Tollon

Garès

et al. 1990

Journal of Cell Science

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The regulation of the mitotic histone H1 kinase activity has been analyzed during the naturally synchronous cell cycle of Physarum polycephalum plasmodia. The universal binding property of the p13suc1 Schizosaccharomyces pombe gene product was used to precipitate and assay the cdc2 histone H1 kinase activity. The kinase activity peaks at the beginning of metaphase and its decline, which requires protein synthesis, appears to be an early event during the metaphase process. Microtubular poisons, temperature shifts and DNA synthesis inhibitors were used to perturb cell cycle regulatory pathways and characterize their effects on cdc2 kinase activation. Our results suggest that the full activation of the mitotic kinase requires at least two successive triggering signals involving microtubular components and DNA synthesis.

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Regulation of tubulin synthesis during the cell cycle in the synchronous plasmodia of Physarum polycephalum

Cited by 5 publications

References 38 publications

A conceptual view at microtubule plus end dynamics in neuronal axons

A conceptual view at microtubule plus end dynamics in neuronal axons

The mammalian iris‐ciliary complex affects organization and synthesis of cytoskeletal protein of organ and tissue cultured lens epithelial cells

Cell cycle regulation of p34 cdc2 kinase activity in Physarum polycephalum

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