BAG-1 accelerates cell motility of human gastric cancer cells

Naishiro, Yasuyoshi; Adachi, Masaaki; Okuda, Hiroyuki; Yawata, Atsushi; Mitaka, Toshihiro; Takayama, Shinichi; Reed, John C.; Hinoda, Yuji; Imai, Kohzoh

doi:10.1038/sj.onc.1202661

Cited by 47 publications

(26 citation statements)

References 28 publications

(35 reference statements)

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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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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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“…BAG-1 is an important regulatory protein that has been shown to have a variety of binding partners and a range of bioactivities, including protection from apoptotic signals (11,19), enhancement of cell motility (20) and regulation of transcription (21,22). BAG-1 has been reported to bind the cytoplasmic domain of the HGF receptor (14), the Raf-1 kinase (23), and several members of the steroid hormone receptor superfamily (21,24), and to be capable of altering the activity of these molecules.…”

Section: Discussionmentioning

confidence: 99%

BAG-1 Is a Novel Cytoplasmic Binding Partner of the Membrane Form of Heparin-binding EGF-like Growth Factor

Lin

Hutchinson

Gaston

et al. 2001

Journal of Biological Chemistry

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Several cell functions related to growth and survival regulation have been attributed specifically to the membrane form of heparin-binding EGF-like growth factor (proHB-EGF), rather than to the diffusible, processed HB-EGF isoform. These findings suggest the existence of a functional binding partner specifically for the membrane form of the growth factor. In this study we have identified the prosurvival cochaperone, BAG-1, as a protein that interacts with the cytoplasmic tail domain of proHB-EGF. Interaction between BAG-1 and the 24-amino acid proHB-EGF cytoplasmic tail was initially identified in a yeast two-hybrid screen and was confirmed in mammalian cells. The proHB-EGF tail bound BAG-1 in an hsp70-independent manner and within a 97-amino acid segment that includes the ubiquitin homology domain in BAG-1 but does not include the hsp70 binding site. Effects of BAG-1 and proHB-EGF co-expression were demonstrated in cell adhesion and cell survival assays and in quantitative assays of regulated secretion of soluble HB-EGF. Because the BAG-1 binding site is not present on the mature, diffusible form of the growth factor, these findings suggest a new mechanism by which proHB-EGF, in isolation from the diffusible form, can mediate cell signaling events. In addition, because effects of BAG-1 on regulated secretion of soluble HB-EGF were also identified, this interaction has the potential to alter the signaling capabilities of both the membrane-anchored and the diffusible forms of the growth factor.

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“…Therefore, the nuclear expression of BAG-1 was impressively correlated with the malignant potential in colorectal cancer. BAG-1 has been reported to facilitate epithelial cell survival following detachment from the underlying extracellular matrix (Ruoslahti, 1996;Weaver et al, 1996) and to promote cell migration in human gastric cancer cells (Naishiro et al, 1999). These functions could contribute to the development of distant metastases in malignant tumours since the overexpression of BAG-1 in melanoma cells increases the metastatic potential of these tumour cells (Takaoka et al, 1997).…”

Section: Molecular and Cellular Pathologymentioning

confidence: 99%

Nuclear BAG-1 expression reflects malignant potential in colorectal carcinomas

et al. 2002

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BAG-1 is a recently identified Bcl-2-interacting anti-apoptotic protein. The aim of our study was to investigate the immunohistochemical staining pattern of BAG-1 protein in patients with colorectal cancer and examine associations of BAG-1 expression with various clinicopathological factors and patient survival. Tumour samples were collected from 86 patients diagnosed with colorectal cancer. There was significant variation in the immunohistochemical staining patterns for BAG-1, including absent staining and staining of either the cytoplasm, nucleus or both. Twenty-one colorectal carcinomas (24.4%) exhibited a nuclear staining pattern whilst 56 (65.1%) exhibited cytoplasmic staining. The percentage of cases exhibiting nuclear BAG-1 positivity was significantly higher in distant metastasis-positive cases (55.6%) than in distant metastasis-negative cases (20.8%; P=0.036). Overall survival was significantly shorter for patients with tumours exhibiting BAG-1 positive nuclei than those with absent nuclear BAG-1-staining (P=0.011). In addition, the multivariate cox proportional hazard models indicated that nuclear BAG-1 expression was the only independent prognostic variable for mortality (P=0.013). These studies demonstrate that nuclear BAG-1 expression is a useful predictive factor for distant metastasis and a poor prognosis in patients with colorectal cancer.

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BAG-1 accelerates cell motility of human gastric cancer cells

Cited by 47 publications

References 28 publications

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

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

BAG-1 Is a Novel Cytoplasmic Binding Partner of the Membrane Form of Heparin-binding EGF-like Growth Factor

Nuclear BAG-1 expression reflects malignant potential in colorectal carcinomas

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