Four and a half LIM domains 1 (FHL1) and receptor interacting protein of 140 kDa (RIP140) interact and cooperate in estrogen signaling

Lin, Jing; Ding, Lei; Jin, Rui; Zhang, Hao; Cheng, Long; Qin, Xi; Chai, Jia-ke; Ye, Qinong

doi:10.1016/j.biocel.2009.02.007

Cited by 37 publications

(29 citation statements)

References 34 publications

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“…Increasing amounts of evidence show that different combinations of LIM domains are responsible for interaction with different proteins. For example, all LIM domains of FHL1 are required to interact with RIP140 (24). Similarly, deletion of any complete LIM domain or the N terminal half domain of FHL2 ablates the interaction with TNF receptor-associated factor 6 (TRAF6) (25).…”

Section: Discussionmentioning

confidence: 99%

FHL family members suppress vascular endothelial growth factor expression through blockade of dimerization of HIF1α and HIF1β

et al. 2012

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SummaryFour and a half LIM domain (FHL) proteins belong to a family of LIM-only proteins that have been implicated in the development and progression of various types of cancers. However, the role of FHL proteins in tumor angiogenesis remains to be elucidated. Herein, we demonstrate that FHL1-3 decrease the promoter activity and expression of vascular endothelial growth factor (VEGF), the key regulator of angiogenesis in cancer growth and progression as well as an important target gene of the transcription factor hypoxia-inducible factor 1 (HIF1a/ HIF1b). FHL1-3 interacted with HIF1a both in vitro and in vivo. A single LIM domain of FHL1 was sufficient for its interaction with HIF1a. FHL1 interacted with the HIF1a region containing basic helix-loop-helix (bHLH) motif and PER-ARNT-SIM domain, both of which aid in dimerization with HIF1b and DNA binding. FHL1-3 inhibited HIF1 transcriptional activity and HIF1-mediated VEGF expression in a hypoxia-independent manner. Moreover, FHL1 blocked HIF1a-HIF1b heterodimerization and HIF1a recruitment to the VEGF promoter. These data suggest that FHL proteins are involved in negative regulation of VEGF possibly by interfering with the dimerization and DNA binding of HIF1 subunits and may play an important role in tumor angiogenesis. Keywords four and a half LIM domain; vascular endothelial growth factor; hypoxia-inducible factor 1; protein-protein interaction; transcriptional activity.

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Section: Discussionmentioning

confidence: 99%

FHL family members suppress vascular endothelial growth factor expression through blockade of dimerization of HIF1α and HIF1β

et al. 2012

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“…RIP140 was first identified as a negative regulator of estrogen receptor signaling [18,19]. More and more studies have found that RIP140 could regulate multiple signal pathways.…”

Section: Discussionmentioning

confidence: 98%

“…The transcription cofactor receptor-interacting protein of 140 kDa (RIP140) is first identified as a partner of estrogen receptor [18,19]. Recent studies have found that RIP140 could interact with lots of nuclear receptors and transcription factors.…”

Section: Introductionmentioning

confidence: 99%

Downregulation of RIP140 in hepatocellular carcinoma promoted the growth and migration of the cancer cells

et al. 2014

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Hepatocellular carcinoma (HCC) is one of the most common malignancies with a poor response to chemotherapy. It is very important to identify novel diagnosis biomarkers and therapeutic targets. RIP140, a regulator of estrogen receptor, recently has been found to be involved in the tumorigenesis. However, its function in the progression of HCC remains poorly understood. Here, we found that the expression of RIP140 was downregulated in the HCC tissues. Moreover, overexpression of RIP140 in HCC cells inhibited cell proliferation and migration, while downregulation of RIP140 promoted the tumorigenicity of HCC cells in vitro and in vivo. Mechanistically, RIP140 interacted with beta-catenin and negatively regulated beta-catenin/TCF signaling. Taken together, our study suggests the suppressive roles of RIP140 in the pathogenesis of HCC.

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“…They also found that FHL proteins ultimately increased the expression of growth inhibitor genes, such as the CDK inhibitor, p21, and that they decreased the expression of the growth-promoting gene, c-myc (17). In addition, FHL1 interacts with estrogen receptors and inhibits breast cancer cell growth (24,25). Moreover, estrogen receptors are highly expressed in BC and contribute to BC cell proliferation (26,27).…”

Section: Discussionmentioning

confidence: 99%

CpG hypermethylation of human four-and-a-half LIM domains 1 contributes to migration and invasion activity of human bladder cancer

Matsumoto

Kawakami²,

Enokida³

et al. 2010

Int J Mol Med

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Abstract. We previously reported a simple technique that combines microarray data from clinical bladder cancer (BC) specimens with those from a BC cell line (BOY) treated with a pharmacologic demethylating agent (5-aza-dC). We focused on the human four-and-a-half LIM domains 1 (FHL1) gene which was selected on the basis of previous microarray data analysis. Because LIM domains provide protein-protein binding interfaces, FHL genes play an important role in cellular events, such as focal adhesion and differentiation, by interacting with the target protein as either a repressor or activator. We hypothesized that inactivation of the FHL1 gene through CpG methylation contributes to cell viability including migration and invasion activity of human BC. After 5-aza-dC treatment, the expression levels of FHL1 mRNA transcript markedly increased in all cell lines tested, as shown by real-time reverse transcription-polymerase chain reaction (RT-PCR). The methylation index of FHL1 in our samples was significantly higher in 70 BC specimens than in 10 normal bladder epithelium (NBE) specimens (63.9±25.5 and 0.3±0.2, respectively; p=0.0066). Conversely, FHL1 mRNA expression was significantly lower in the BC specimens than in the NBE ones (0.331±0.12 and 2.498±0.61, respectively; p=0.0011). In addition, significant inhibitions of wound healing (45.78±6.2, and 100±0, respectively; p=0.009) and of cell invasion (18.5±2.3 and 95.2±2.4, respectively; p=0.02) were observed in stable FHL1-transfected cells than in the control BC cells. In conclusion, we found that the mechanism of FHL1 down-regulation in BC is through CpG hypermethylation of the promoter region. FHL1 gene inactivation by CpG hypermethylation may thus contribute to migration and invasion activity of BC.

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Four and a half LIM domains 1 (FHL1) and receptor interacting protein of 140 kDa (RIP140) interact and cooperate in estrogen signaling

Cited by 37 publications

References 34 publications

FHL family members suppress vascular endothelial growth factor expression through blockade of dimerization of HIF1α and HIF1β

FHL family members suppress vascular endothelial growth factor expression through blockade of dimerization of HIF1α and HIF1β

Downregulation of RIP140 in hepatocellular carcinoma promoted the growth and migration of the cancer cells

CpG hypermethylation of human four-and-a-half LIM domains 1 contributes to migration and invasion activity of human bladder cancer

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