Identification and characterization of FHL3 as a novel angiogenin-binding partner

Xia, Wenrong; Fu, Wenliang; Cai, Ling; Kong, Haibo; Cai, Xiaoyan; Liu, Jing; Wang, Yuanyuan; Zou, Minji; Xu, Donggang

doi:10.1016/j.gene.2012.05.019

Cited by 9 publications

(9 citation statements)

References 29 publications

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“…FHL3 has been previously identified as a novel angiogenin (Ang) binding partner. Furthermore, FHL3 was required for Ang-mediated HeLa cell proliferation and the nuclear translocation of Ang, a finding that highlights FHL3 as a potential candidate involved in the molecular mechanisms behind the antiapoptotic property of cancer cells (44). Our experiments show that FHL3 may induce caspase-3-mediated apoptosis in gliomas.…”

Section: Discussionsupporting

confidence: 53%

RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3

Han¹,

Xin²,

Zhao³

et al. 2013

J. Clin. Invest.

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Section: Discussionsupporting

confidence: 53%

RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3

Han¹,

Xin²,

Zhao³

et al. 2013

J. Clin. Invest.

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“…proteins [60,61] and cytoskeletal proteins [56,62,63]; (ii) cell proliferation, including follistatin [52,64], phospholipid scramblase 1 (PLSCR1) [57], histone H3 [65], RNH1 [50], four and a half LIM domains 3 (FHL3) [54,66], and ANG receptor that is a 170-kDa cellsurface protein expressed in human endothelial cells [67] or syndecan 4 in astrocyte cells [59]; and (iii) cell apoptosis, including p53 [51], MDM2 [51], heat shock factor 1 (HSF1) [58], and RNH1 [50]. A full identification of ANG-interacting proteins may help to draw the ANG interaction maps and to better understand its roles and mechanisms.…”

Section: Ang-interacting Proteinsmentioning

confidence: 99%

Three decades of research on angiogenin: a review and perspective

Sheng¹,

Xu²

2016

ABBS

179

201

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As a member of the vertebrate-specific secreted ribonucleases, angiogenin (ANG) was first isolated and identified solely by its ability to induce new blood vessel formation, and now, it has been recognized to play important roles in various physiological and pathological processes through regulating cell proliferation, survival, migration, invasion, and/or differentiation. ANG exhibits very weak ribonucleolytic activity that is critical for its biological functions, and exerts its functions through activating different signaling transduction pathways in different target cells. A series of recent studies have indicated that ANG contributes to cellular nucleic acid metabolism. Here, we comprehensively review the results of studies regarding the structure, mechanism, and function of ANG over the past three decades. Moreover, current problems and future research directions of ANG are discussed. The understanding of the function and mechanism of ANG in a wide context will help to better delineate its roles in diseases, especially in cancer and neurodegenerative diseases.

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“…Recently, FHL3 has been shown to play roles in carcinogenesis [8]–[12]. However, the detailed mechanisms of its actions are still not well-defined.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, FHL3 is involved in the development and progression of breast cancer by suppressing breast cancer cell growth and inducing cell-cycle arrest [11]. Furthermore, our previous study has demonstrated that FHL3 is required for Ang-mediated HeLa cell proliferation by inhibiting nuclear translocation of Ang, suggesting that it may also play an important role in Ang-regulated cancer cell growth and apoptosis [12].…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of MT-1X as a Novel FHL3-Binding Partner

Cai¹,

Wang²,

Huang³

et al. 2014

PLoS ONE

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Four and a half LIM domain protein 3 (FHL3) is a member of the FHL protein family that plays roles in the regulation of cell survival, cell adhesion and signal transduction. However, the mechanism of action for FHL3 is not yet clear. The aim of present study was to identify novel binding partner of FHL3 and to explore the underlying mechanism. With the use of yeast two-hybrid screening system, FHL3 was used as the bait to screen human fetal hepatic cDNA library for interacting proteins. Methionine-1X was identified as a novel FHL3 binding partner. The interaction between FHL3 and the full length MT-1X was further confirmed by yeast two-hybrid assay, co-immunoprecipitation and GST pull-down assays. Furthermore,the result demonstrated that MT-1X knockdown promoted the FHL3-induced inhibitory effect on HepG2 cells by regulating FHL3-mediated Smad signaling and involving in the modulation the expression of G2/M phase-related proteins through interaction with FHL3. These findings suggest that functional interactions between FHL3 and MT-1X may provide some clues to the mechanisms of FHL3-regulated cell proliferation.

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Identification and characterization of FHL3 as a novel angiogenin-binding partner

Cited by 9 publications

References 29 publications

RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3

RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3

Three decades of research on angiogenin: a review and perspective

Identification and Characterization of MT-1X as a Novel FHL3-Binding Partner

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