Interaction of BAG-1 with Retinoic Acid Receptor and Its Inhibition of Retinoic Acid-induced Apoptosis in Cancer Cells

Liu, Ru; Takayama, Shinichi; Zheng, Yun; Froesch, Barbara A.; Chen, Guoquan; Zhang, Xin; Reed, John C.; Zhang, Xiaokun

doi:10.1074/jbc.273.27.16985

Cited by 114 publications

(85 citation statements)

References 43 publications

(68 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…[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

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

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

et al. 2005

View full text Add to dashboard Cite

show abstract

“…33,34 In addition to Hsp70, BAG proteins also bind to cell surface receptors. Interaction of Bag-1M isoform in concert with Hsp70/Hsc70 to retinoic acid receptors, glucocorticoid, estrogen, and thyroid hormone receptors [33][34][35][36] mediates stress signaling pathways that regulate Raf-1/ERK c-Irradiation and Hsp70/Bag-4/Hsp40 membrane expression M Gehrmann et al and cell growth. 37 Bag-3 forms an EGF-regulated ternary complex with phospholipase C-g and Hsp/70/Hsc70 in human melanoma cells.…”

Section: Discussionmentioning

confidence: 99%

Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells

et al. 2004

View full text Add to dashboard Cite

CX þ /CXÀ and Colo þ /ColoÀ tumor sublines with stable heat shock protein 70 (Hsp70) high and low membrane expression were generated by fluorescence activated cell sorting of the parental human colon (CX2) and pancreas (Colo357) carcinoma cell lines, using an Hsp70-specific antibody. Two-parameter flow cytometry revealed that Hsp70 colocalizes with Bag-4, also termed silencer of death domain, not only in the cytosol but also on the plasma membrane. After nonlethal c-irradiation, the percentage of membranepositive cells and the protein density of Hsp70 and Bag-4 were found to be strongly upregulated in carcinoma sublines with initially low expression levels (CXÀ, ColoÀ). Membrane expression of Hsp70 was also elevated in Bag-4 overexpressing HeLa cervix carcinoma cells when compared to neo-transfected cells. In response to c-irradiation, neotransfected HeLa cells behaved like Hsp70/Bag-4 lowexpressing CXÀ and ColoÀ, and Bag-4-transfected HeLa cells like Hsp70/Bag-4 high-expressing carcinoma sublines CX þ and Colo þ . Immunoprecipitation studies further confirmed colocalization of Hsp70 and Bag-4 but also point to an association of Hsp70 and Hsp40 on the plasma membrane of CX þ and Colo þ cells; on CXÀ and ColoÀ tumor sublines, Hsp40 was detectable in the absence of Hsp70 and Bag-4. Other co-chaperones including Hsp60 and Hsp90 were neither found on the cell surface of CX þ /CXÀ, Colo þ /ColoÀ nor on HeLa neo-/HeLa Bag-4-transfected tumor cells. Functionally, Hsp70/Bag-4 and Hsp70/Hsp40 membrane-positive tumor cells appeared to be better protected against radiation-induced effects, including G2/M arrest and growth inhibition, on the one hand. On the other hand, membrane-bound Hsp70, but neither Bag-4 nor Hsp40, served as a recognition site for the cytolytic attack mediated by natural killer cells.

show abstract

“…BAG-1 can promote Ras-independent activation of Raf-1 kinase (Wang et al, 1996). Moreover, BAG-1 modulates the activities of the p53-inducible factor Siah-1 and some steroid hormone receptors (Matsuzawa et al, 1998), promoting cell growth and survival and conferring resistance to retinoids and antiandrogens (Liu et al, 1998;Kullmann et al, 1998). Thus, multiple functions have been attributed to BAG-1, and essentially all of these could contribute to malignant cell behaviors.…”

Section: Introductionmentioning

confidence: 99%

BAG-1 accelerates cell motility of human gastric cancer cells

et al. 1999

Self Cite

View full text Add to dashboard Cite

Interaction of BAG-1 with Retinoic Acid Receptor and Its Inhibition of Retinoic Acid-induced Apoptosis in Cancer Cells

Cited by 114 publications

References 43 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

Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells

BAG-1 accelerates cell motility of human gastric cancer cells

Contact Info

Product

Resources

About