Review: Nuclear Events in Apoptosis

Review: Nuclear Events in Apoptosis Initial apoptosis research characterized this form of cell death based on distinct nuclear morphology that was subsequently shown to be associated with the appearance of oligonucleosomal DNA fragments. More recent evidence has indicated that apoptosis depends upon a tightly regulated cellular program for its successful initiation and execution. Molecular participants in this program are present in different subcellular compartments, including the plasma membrane, cytosol, mitochondria, and nucleus. The interplay among these compartments and the exchange of specific signaling molecules are critical for the systematic progression of apoptosis. While numerous reports have described a key role for caspase activity in the signaling and executive steps of apoptotic cell death, there are some instances where well-established nuclear changes, characteristic of this form of cell death, can occur independently of caspase activity. Moreover, evidence indicates that certain nuclear events, including chromatin condensation and DNA fragmentation, are controlled separately and depend upon a persistent supply of energy in vivo. In this review, we discuss our current understanding of the role and regulation of nuclear events in the apoptotic process with an emphasis on protease and endonuclease activities as well as the ability of certain Bcl-2 family proteins to influence this process. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Structural Biology Elsevier

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Publisher
Elsevier
Copyright
Copyright © 2000 Academic Press
ISSN
1047-8477
eISSN
1095-8657
DOI
10.1006/jsbi.2000.4254
Publisher site
See Article on Publisher Site

Abstract

Initial apoptosis research characterized this form of cell death based on distinct nuclear morphology that was subsequently shown to be associated with the appearance of oligonucleosomal DNA fragments. More recent evidence has indicated that apoptosis depends upon a tightly regulated cellular program for its successful initiation and execution. Molecular participants in this program are present in different subcellular compartments, including the plasma membrane, cytosol, mitochondria, and nucleus. The interplay among these compartments and the exchange of specific signaling molecules are critical for the systematic progression of apoptosis. While numerous reports have described a key role for caspase activity in the signaling and executive steps of apoptotic cell death, there are some instances where well-established nuclear changes, characteristic of this form of cell death, can occur independently of caspase activity. Moreover, evidence indicates that certain nuclear events, including chromatin condensation and DNA fragmentation, are controlled separately and depend upon a persistent supply of energy in vivo. In this review, we discuss our current understanding of the role and regulation of nuclear events in the apoptotic process with an emphasis on protease and endonuclease activities as well as the ability of certain Bcl-2 family proteins to influence this process.

Journal

Journal of Structural BiologyElsevier

Published: Apr 1, 2000

References

  • Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death
    Casciola-Rosen, L.; Nicholson, D.W.; Chong, T.; Rowan, K.R.; Thornberry, N.A.; Miller, D.K.; Rosen, A.
  • CPAN, a human nuclease regulated by the caspase-sensitive inhibitor DFF45
    Halenbeck, R.; MacDonald, H.; Roulston, A.; Chen, T.T.; Connroy, L.; Williams, L.T.
  • Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis
    Hirata, H.; Takahashi, A.; Kobayashi, S.; Yonehara, S.; Sawai, H.; Okazaki, T.; Yamamoto, K.; Sasada, M.
  • CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor
    Inohara, N.; Koseki, T.; Chen, S.; Wu, X.; Nunez, G.
  • Cytosolic nuclease activated by caspase-3 in inhibited by DFF-45
    Mitamura, S.; Ikawa, H.; Mizuno, N.; Kaziro, Y.; Itoh, H.
  • Lamin proteolysis facilitates nuclear events during apoptosis
    Rao, L.; Perez, D.; White, E.
  • Apoptotic nuclear morphological change without DNA fragmentation
    Sakahira, H.; Enari, M.; Ohsawa, Y.; Uchiyama, Y.; Nagata, S.
  • Cell nucleus and DNA fragmentation are not required for apoptosis
    Schulze-Osthoff, K.; Walczak, H.; Droge, W.; Krammer, P.H.
  • Purification of three cytotoxic lymphocyte granule serine proteases that induce apoptosis through distinct substrate and target cell interaction
    Shi, L.; Kam, C.M.; Powers, J.C.; Aebersold, R.; Greenberg, A.H.
  • Granzyme B (GraB) autonomously crosses the cell membrane and perforin initiates apoptosis and GraB nuclear localization
    Shi, L.; Mai, S.; Israels, S.; Browne, K.; Trapani, J.A.; Greenberg, A.H.
  • DEDD, a novel death effector domain-containing protein, targeted to the nucleolus
    Stegh, A.H.; Schickling, O.; Ehret, A.; Scaffidi, C.; Peterhansel, C.; Hofmann, T.G.; Grummt, I.; Krammer, P.H.; Peter, M.E.
  • Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs)
    Torii, S.; Egan, D.A.; Evans, R.A.; Reed, J.C.
  • Intracellular acidification during apoptosis can occur in the absence of a nucleus
    Wolf, C.M.; Eastman, A.
  • Essential role of active nuclear transport in apoptosis
    Yasuhara, N.; Eguchi, Y.; Tachibana, T.; Imamoto, N.; Yoneda, Y.; Tsujimoto, Y.
  • Two different proteases are involved in the proteolysis of lamin during apoptosis
    Zhivotovsky, B.; Gahm, A.; Orrenius, S.

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