Activation of polyubiquitin gene expression during developmentally programmed cell death

@article{Schwartz1990ActivationOP,
  title={Activation of polyubiquitin gene expression during developmentally programmed cell death},
  author={Lawrence M Schwartz and Anita Myer and L Kosz and Marcy Engelstein and Caroline Maier},
  journal={Neuron},
  year={1990},
  volume={5},
  pages={411-419}
}

Post-transcriptional regulation of gene expression during the programmed death of insect skeletal muscle

TLDR
Data suggest that there may be global removal of cellular transcripts just prior to death to allow newly expressed mRNAs to rapidly accumulate to high levels and facilitate the efficient activation of death (and perhaps other differentiation programs) in some developmental systems.

Developmental Changes of the 26 S Proteasome in Abdominal Intersegmental Muscles of Manduca sexta during Programmed Cell Death (*)

TLDR
A large increase in the concentration of 26 S proteasomes together with extensive regulatory reprogramming may facilitate rapid muscular proteolysis.

Regulation of apoptosis by ubiquitination

TLDR
This review focuses on the direct effects of ubiquitination on apoptosis‐signaling molecules and reports of polyubiquitin conjugation of key pro‐ and anti‐apoptotic molecules as an essential regulatory modification targeting proteins for proteasomal degradation.

The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating enzyme involved in selective protein degradation

TLDR
Cl cloning and characterization of a gene (ubc-2) encoding a ubiquitin-conjugating enzyme which is involved in the selective degradation of abnormal and short-lived proteins in the nematode Caenorhabditis elegans suggest that yeast UBC4 and UBC5, Drosophila UbcD1, and C. elegans ubc-2 define a highly conserved gene family which plays fundamental roles in all eukaryotic cells.

Role of ubiquitin conjugating enzymes in Drosophila development

TLDR
The role of the ubiquitin system in development is addressed using Drosophila melanogaster as a model system, with particular developmental roles for the E2 genes suggested, as RNA from all known E2s was found to be abundant in this tissue in embryos.

Links between the Ubiquitin-Proteasome System and Cell Death Pathways in Arabidopsis thaliana

TLDR
It could be shown that exposure to additional, normally harmless stress factors is able to accelerate the cell death process, and the isolation and characterization of suppressor of UbK48R-induced cell death (sud) mutants indicated changes in distinct, rather specialized pathways.

Ubiquitin in homeostasis, development and disease

  • S. MullerL. Schwartz
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1995
TLDR
While the ubiquitin/26S proteasome pathway is responsible for the degradation of the bulk of cellular proteins during homeostasis, it may also beresponsible for the rapid loss of protein during the programmed death of certain cells, such as skeletal muscle during insect metamorphosis.

Localization of immunoreactive ubiquitin in the nervous system of the Manduca sexta moth

TLDR
Investigation of the adbominal gaglia of Manduca sexta suggests that this protein plays a number of important roles in neuronal physiology and may be associated with the death of some neurons in this tissue, and the most intense staining of neuronal cytoplasm was found not in dying neurons, but in sets of persisting neurons that may serve a primarily neurosecretory or neuromodulatory function.

The role of cell death genes during development

  • L. Schwartz
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1991
TLDR
Accumulation of ubiquitin has been observed not only during programmed cell death, but also in several neurodegenerative disorders, including Alzheimer's Disease.
...

References

SHOWING 1-10 OF 35 REFERENCES

Gene activation is required for developmentally programmed cell death.

TLDR
The data presented here indicate that programmed cell death is not due to the cessation of macromolecular synthesis in condemned cells but rather is due toThe activation of a differentiative pathway.

Ubiquitin-mediated protein degradation.

  • A. Hershko
  • Biology
    The Journal of biological chemistry
  • 1988

An ancient developmental induction: heat-shock proteins induced in sporulation and oogenesis.

TLDR
A strikingly similar pattern of expression occurs during oogenesis in Drosophila, suggesting that it may be one of the earliest developmental pathways to evolve in eukaryotic cells.

Degradation of proteins with acetylated amino termini by the ubiquitin system

TLDR
The results suggest that a novel conjugating enzyme (possibly a ubiquitin-protein ligase) may be responsible for the degradation of these acetylated proteins by recognizing structural features of the substrate that are downstream and distinct from the NH2-terminal residue.

Cascade induction of c-fos, c-myc, and heat shock 70K transcripts during regression of the rat ventral prostate gland.

TLDR
Analysis of RNA extracted from regressing ventral prostate glands showed that the c-fos gene was induced at 36 h, earlier than c-myc, alpha-tubulin, and hsp 70, and later, during the most active period of cell death, their expression was transiently induced.

The yeast ubiquitin genes: a family of natural gene fusions.

TLDR
itin genes are expressed in exponentially growing cells, while in stationary‐phase cells the expression of UB11 and UB12 is repressed, and it is shown that the essential function of the UB14 gene is to provide ubiquitin to cells under stress.

Cell death in embryogenesis

TLDR
The process of rudimentation — organ or tissue regression (whether phylogenetic or morphogenetic) and its control — has recently been extensively reviewed in a congress report (Raynaud, 1977a).