p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1

Matsuzawa, Shu‐ichi; Takayama, Shinichi; Froesch, Barbara A.; Zapata, Juán M.; Reed, John C.

doi:10.1093/emboj/17.10.2736

Cited by 194 publications

(177 citation statements)

References 57 publications

(94 reference statements)

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“…Using epitope-tagged protein, cellular localization of SIAH-1 was reported as predominantly cytoplasmic (Hu et al, 1997) or nucleic (Matsuzawa et al, 1998). It was also shown that the ring domain of the protein was required for the formation of punctuated structures in the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

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SIAH-1 inhibits cell growth by altering the mitotic process

et al. 1999

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SIAH-1, the human homologue of the drosophila seven in absentia gene, is a p53-p21 Waf-1 inducible gene. We report that stable transfection with SIAH-1 of the epithelial breast cancer cell line MCF-7 blocks its growth process. The transfectants show a redistribution of SIAH-1 protein within the nucleus, more speci®cally to the nuclear matrix, associated to dramatic changes in cell morphology and defective mitosis. Multinucleated giant cells (2 ± 12 nuclei in more than 50% cells) were a most striking observation associated with tubulin spindle disorganization and defective cytokinesis. There were also present at high frequency abortive mitotic ®gures, DNA bridges and persistance of intercellular bridges and midbodies, along with an increased expression of p21 Waf-1 . These results indicate that the mechanism of growth arrest induced by SIAH-1 in MCF-7 cells involves disorganization of the mitotic program, mainly during nuclei separation and cytokinesis.

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Section: Discussionmentioning

confidence: 99%

“…SIAH-1 binds Bag-1 protein and inhibits cell growth (Matsuzawa et al, 1998). Bag-1 is a widely expressed protein with an ubiquitin-like domain that binds and cooperates with Bcl-2 in suppressing cell death.…”

Section: Introductionmentioning

confidence: 99%

SIAH-1 inhibits cell growth by altering the mitotic process

et al. 1999

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“…[60][61][62][63][64][65][66][67][68][69] The functional diversity of BAG domain proteins is paralleled by an abundance of genes of this family throughout evolution, with homologs identified in a variety of organisms, including yeast, worm, invertebrates, amphibians, mammals, and plants. 21,59,60,70 Database searches indicate the presence of eight genes that encode proteins with the BAG domain in Arabidopsis thaliana.…”

Section: Discussionmentioning

confidence: 99%

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

et al. 2005

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Calmodulin (CaM) influences many cellular processes by interacting with various proteins. Here, we isolated AtBAG6, an Arabidopsis CaM-binding protein that contains a central BCL-2-associated athanogene (BAG) domain. In yeast and plants, overexpression of AtBAG6 induced cell death phenotypes consistent with programmed cell death (PCD). Recombinant AtBAG6 had higher affinity for CaM in the absence of free Ca 2 þ than in its presence. An IQ motif (IQXXXRGXXXR, where X denotes any amino-acid) was required for Ca 2 þ -independent CaM complex formation and single amino-acid changes within this motif abrogated both AtBAG6-activated CaM-binding and cell death in yeast and plants. A 134-amino-acid stretch, encompassing both the IQ motif and BAG domain, was sufficient to induce cell death. Agents generating oxygen radicals, which are known to be involved in plant PCD, specifically induced the AtBAG6 transcript. Collectively, these results suggest that AtBAG6 is a stress-upregulated CaM-binding protein involved in plant PCD.

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“…Firstly, p53-induced SIAH expression may participate in the phosphorylation-independent degradation of bcatenin; however, its relevance in HCCs has not been shown until now (Matsuzawa et al, 1998;Liu et al, 2001a;Matsuzawa and Reed, 2001). Secondly, accumulation of b-catenin wt correlates positively with a high exposure of aflatoxin B1 (Devereux et al, 2001) and with mutational inactivation of p53 in HCCs (Cagatay and Ozturk, 2002); however, a direct connection between all three parameters (aflatoxin intoxication, aflatoxin-specific G/T mutation in p53 mut/249 and bcatenin enrichment) has not been shown so far.…”

Section: Cross-talk With Protumorigenic Factorsmentioning

confidence: 99%