Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis.

Bonneau, A M; Sonenberg, Nahum

doi:10.1016/s0021-9258(18)60935-4

Cited by 208 publications

(17 citation statements)

References 31 publications

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“…Ironically, the simplest explanation is that mitosis is both destructive and stressful for the dividing cell, and is therefore a process best finished quickly. During mitosis, among other things, the nuclear envelope is torn apart (Gerace et al, 1978), the Golgi and ER membrane systems undergo dramatic reorganization (Hetzer, 2010;Robbins and Gonatas, 1964), vesicle trafficking ceases (Sager et al, 1984), chromosomes condense and transcription is disabled (Taylor, 1960;Prescott and Bender, 1962), translation is slowed (Prescott and Bender, 1962;Bonneau and Sonenberg, 1987), and both the actin and microtubule cytoskeletons are reshaped to facilitate cell rounding and assembly of the bipolar mitotic spindle (Saxton et al, 1984;Kunda and Baum, 2009). Such dramatic perturbations to the normal cellular architecture during mitosis cannot be tolerated indefinitely, and we are just beginning to understand the consequences of extending such an abnormal state: the infrastructure of mitotic chromosomes, slowly but surely, begins to break down during prolonged mitosis, ultimately giving rise to DNA breaks.…”

Section: The Damaging Effects Of Prolonged Mitosismentioning

confidence: 99%

Linking abnormal mitosis to the acquisition of DNA damage

Ganem

Pellman

2012

Journal of Cell Biology

183

153

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Cellular defects that impair the fidelity of mitosis promote chromosome missegregation and aneuploidy. Increasing evidence reveals that errors in mitosis can also promote the direct and indirect acquisition of DNA damage and chromosome breaks. Consequently, deregulated cell division can devastate the integrity of the normal genome and unleash a variety of oncogenic stimuli that may promote transformation. Recent work has shed light on the mechanisms that link abnormal mitosis with the development of DNA damage, how cells respond to such affronts, and the potential impact on tumorigenesis.

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Section: The Damaging Effects Of Prolonged Mitosismentioning

confidence: 99%

Linking abnormal mitosis to the acquisition of DNA damage

Ganem

Pellman

2012

Journal of Cell Biology

183

153

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“…During the archetypal cell cycle, cap-dependent translation peaks in G1 phase and decreases by 60-80% in mitosis, when cellular energy is mostly invested into ensuring accurate cell division [45,46,65]. Genome-wide polysome profiling showed that approximately 3 per cent of HeLa cell mRNAs, encoding mostly nuclear RNA-binding proteins, efficiently associate with actively translating polysomes in mitosis [66].…”

Section: (A) G1 -S Transitionmentioning

confidence: 99%

Translational regulation of the cell cycle: when, where, how and why?

Kronja

Orr‐Weaver

2011

Phil. Trans. R. Soc. B

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Translational regulation contributes to the control of archetypal and specialized cell cycles, such as the meiotic and early embryonic cycles. Late meiosis and early embryogenesis unfold in the absence of transcription, so they particularly rely on translational repression and activation of stored maternal mRNAs. Here, we present examples of cell cycle regulators that are translationally controlled during different cell cycle and developmental transitions in model organisms ranging from yeast to mouse. Our focus also is on the RNA-binding proteins that affect cell cycle progression by recognizing special features in untranslated regions of mRNAs. Recent research highlights the significance of the cytoplasmic polyadenylation element-binding protein (CPEB). CPEB determines polyadenylation status, and consequently translational efficiency, of its target mRNAs in both transcriptionally active somatic cells as well as in transcriptionally silent mature Xenopus oocytes and early embryos. We discuss the role of CPEB in mediating the translational timing and in some cases spindle-localized translation of critical regulators of Xenopus oogenesis and early embryogenesis. We conclude by outlining potential directions and approaches that may provide further insights into the translational control of the cell cycle.

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“…On the one hand, the modifications almost certainly are sufficient to produce severe protein synthesis inhibition based on in vitro assays (Matts and London, 1984;Clemens et al, 1982). Observations made in vivo correlate such changes with inhibition of protein synthesis induced by serum depletion (Duncan and Hershey, 1985), serum removal , amino acid depletion (Clemens et al, 1987), or mitosis (Bonneau and Sonenberg, 1987). Furthermore, an inhibitory role for eIF-2ct phosphorylation by the double-stranded RNA-regulated eIF-2ct kinase has been demonstrated in vivo by using cells transfected with a cDNA encoding a mutant form of eIF-2tx that cannot be phosphorylated (Kaufman et al, 1989).…”

Section: Covalent Modification Changes During Heat Stress and Restorationmentioning

confidence: 99%

Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation.

Duncan

Hershey

1989

The Journal of Cell Biology

185

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Abstract. Incubating cells at elevated temperaturescauses an inhibition of protein synthesis. Mild heat stress at 41-42°C inhibits the fraction of active, polysomal ribosomes from >60% (preheating) to <30%. A return to 37°C leads to an increase in protein synthesis, termed "recovery." Continuous incubation at 41--420C also leads to a gradual restoration of protein synthesis (>70% of ribosomes reactivated by 2-4 h), termed "adaptation: Protein synthesis inhibition and reactivation in prestressed, recovered cells that contain elevated levels of the heat stress proteins occur to the same extent and at the same rate as in "naive" cells. The adaptation response requires transcription of new RNA whereas recovery does not. A large number of phosphorylation changes are induced by severe heat stress and occur with kinetics similar to the inhibition of protein synthesis. These include phosphorylation of eukaryotic protein synthesis initiation factor (elF)-2c~ and dephosphorylation of elF-4B and elF-4Fp25 (elF-4E). However, the extent to which the modification occurs is proportional to the severity of the stress, and, under mild (41-42°C) heat stress conditions, these initiation factor phosphorylation changes do not occur. Similarly, under conditions of severe heat stress elF2or and elF-4B frequently recover to their prestress phosphorylation state before the recovery of protein synthesis, elF-4E dephosphorylation likewise does not occur under mild heat stress conditions. Therefore, these changes in phosphorylation states, which are thought to be sufficient cause, are not necessary for the inhibition of protein synthesis observed.

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Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis.

Cited by 208 publications

References 31 publications

Linking abnormal mitosis to the acquisition of DNA damage

Linking abnormal mitosis to the acquisition of DNA damage

Translational regulation of the cell cycle: when, where, how and why?

Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation.

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