Removal of proteasomes from the nucleus and their accumulation in apoptotic blebs during programmed cell death

  title={Removal of proteasomes from the nucleus and their accumulation in apoptotic blebs during programmed cell death},
  author={Frank Pitzer and Ada Dantes and Thomas Fuchs and Wolfgang Baumeister and Abraham Amsterdam},
  journal={FEBS Letters},

Intracellular localization of proteasomes.

The role of the ubiquitin-proteasome pathway in apoptosis

This review provides a summary of the experimental basis by which components of the ubiquitin-proteasome pathway have been linked to apoptosis, and attempts are made to formulate a hypothesis about its role in this process.

Autophagy Regulates the Post-Translational Cleavage of BCL-2 and Promotes Neuronal Survival

The cellular content of BCL-2 is regulated at post-translational level along the autophagy/lysosome pathways in organotypic cultures of post-natal mouse cerebellar cortex in order to understand the pivotal role of calcium release from intracellular stores in CGC neuroprotection.

Proteasome Involvement and Accumulation of Ubiquitinated Proteins in Cerebellar Granule Neurons Undergoing Apoptosis

The finding that the proteasomes are early involved in apoptosis and that ubiquitinated proteins accumulate during this process prospect granule neurons as a model system aimed at correlating these events with neurodegenerative diseases is found.

Rho GTPase signalling pathways in the morphological changes associated with apoptosis

This review will discuss how Rho GTPase signalling pathways affect the structure of the actin cytoskeleton and allow for the efficient clearance of apoptotic cells.

Actin depolymerization and polymerization are required during apoptosis in endothelial cells

It is suggested that the actin network of flattened cells is disrupted concomitantly to the morphological modifications associated to the apoptotic cell death, and that the cytochalasin‐sensitive reorganisation of actin is required to the formation of apoptotic blebs.

Apoptotic Membrane Blebbing Is Regulated by Myosin Light Chain Phosphorylation

The model system described here should facilitate future studies of MLCK, Rho, and other signal transduction pathways activated during the execution phase of apoptosis and also implicate Rho signaling in these active morphological changes.


The data of the present study suggest that cAMP may activate apoptosis in granulosa cells by shifting the ratio of the death promoter to death repressor genes via alteration of P53 and bax expression.



Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control.

Since proteasome accumulation appears to coincide with disappearance of cyclins A and B1 from the spindle apparatus, it is suggested that proteasomes may play a role in termination of mitosis by degrading the cyclins, which act as regulatory elements.

Proteolysis of Fodrin (Non-erythroid Spectrin) during Apoptosis (*)

It is demonstrated that cleavage of α-fodrin (non-erythroid spectrin) accompanies apoptosis, induced by activation via the CD3/T cell receptor complex in a murine T cell hybridoma, ligation of the Fas molecule on a human T cell lymphoma line and other Fas-expressing cells, or treatment of cells with staurosporine, dexamethasone, or synthetic ceramide.

Ubiquitin pathway involvement in human lymphocyte gamma-irradiation-induced apoptosis

Evidence is presented that the ubiquitin gene is one of the genes with induced activity in the apoptotic death program and that ubiquitination of nuclear proteins might be involved in chromatin disorganization and oligonucleosomal fragmentation, which are among the key events occurring in apoptosis.

Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death).

The tissue distribution of DNase I is extended to tissues with no digestive function and to cells which are known to be susceptible to apoptosis by proposing that during apoptosis, an endonuclease indistinguishable fromDNase I gains access to the nucleus due to the breakdown of the ER and the nuclear membrane.

Mechanisms and genes of cellular suicide

Genetic studies in the nematode Caenorhabditis elegans and in the fruit fly Drosophila melanogaster have led to the isolation of genes that are specifically required for the induction of programmed cell death.

The molecular biology of apoptosis.

  • D. VauxA. Strasser
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
A molecular understanding of this mechanism may allow design of therapies that either enhance or block cell death at will, and in some circumstances this allows independent regulation of pathways that converge upon a common end point.

Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.

Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway.

It is found that wild-type p53 accumulates markedly because of decreased breakdown when cells are shifted to the restrictive temperature and introduction of sequences encoding the human ubiquitin-activating enzyme E1 corrects the temperature sensitivity defect in ts20 and prevents accumulation of p53.

Involvement of p53 expression in cAMP-mediated apoptosis in immortalized granulosa cells.

Findings demonstrate that wild-type p53 can cooperate with cAMP-generated signals in the induction of steroidogenesis and of programmed cell death in granulosa cells.

Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells.

  • A. RivettA. PalmerE. Knecht
  • Biology
    The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
  • 1992
F affinity-purified antibodies against rat liver MCP were used to investigate the localization of the proteinase both in rat liver and in growing human L-132 cells in culture, using electron microscopic immunogold techniques.