Toward an understanding of the protein interaction network of the human liver

Wang, Jian; Huo, Keke; Ma, Lixin; Tang, Liujun; Liu, Dong; Huang, Xiaobi; Yuan, Yanzhi; Li, Chunhua; Wang, Wei; Guan, Wei; Chen, Hui; Jin, Chaozhi; Wei, Juncheng; Zhang, Wanqiao; Yang, Yongsheng; Liu, Qiongming; Zhou, Ying; Zhang, Cuili; Wu, Zhihao; Xu, Wenjian; Zhang, Ying; Liu, Tao; Yu, Donghui; Zhang, Yaping; Chen, Liang; Zhu, Dewu; Zhong, Xing; Kang, Lixin; Gan, Xiang; Yu, Xiaolan; Ma, Qi; Yan, Jing; Zhou, Li; Liu, Zhongyang; Zhu, Yunping; Zhou, Tao; He, Fuchu; Yang, Xiaoming

doi:10.15252/msb.20178107

Cited by 27 publications

(24 citation statements)

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“…Previous report has suggested the C6orf106 might bind with RPSA [2], and a large number of studies confirmed that RPSA was overexpressed in a variety of malignant tumors, and associated with poor prognosis [3][4][5][6][7][8][9][10][11][12][13][14]. RPSA can downregulate the expression of P21 and upregulate the expression of cyclin A2 and cyclin B1, thereby promoting the fibrosarcoma cell proliferation [18].…”

Section: Discussionmentioning

confidence: 99%

“…So far, the function of C6orf106 in human tissues, tumors, and other diseases is still poorly understood. A high-throughput two-hybrid study predicted that C6orf106 could combine with ribosomal protein SA (RPSA) [2]. RPSA was highly expressed in the colon cancer, breast cancer, ovarian cancer, and other malignant cancers [3][4][5][6], and significantly associated with the proliferation, invasion, and metastasis of tumor [7][8][9][10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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A novel biomarker C6orf106 promotes the malignant progression of breast cancer

Jiang

Zhang

et al. 2015

Tumor Biol.

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C6orf106 (chromosome 6 open reading frame 106) is a recently discovered protein encoded by the 6th chromosome. Though many proteins encoded by chromosome 6 are reportedly related to cancer, schizophrenia, autoimmunity and many other diseases, the function of C6orf106 was not well demonstrated so far. As measured by immunohistochemical staining, C6orf106 was positive in normal breast duct myoepithelial cells (92.31 %, 72/78), but negative in normal breast duct glandular epithelial cells (3.85 %, 3/78). In breast ductal carcinoma in situ, C6orf106 showed weakly or moderately positive (77.97 %, 46/59), but it was significantly strongly positive in invasive ductal carcinoma (79.57 %, 148/186). The expression intensity of C6orf106 seemed increased significantly along with the malignancy of breast cancer (p < 0.001). Additionally, C6orf106 expression was significantly correlated with TNM stage (p = 0.001 and p = 0.004) and lymph node metastasis (p = 0.018 and p = 0.025) of the overall and the triple-negative breast cancer, respectively. Consistently, we found that the interference of C6orf106 was able to inhibit cell proliferation and invasion of two triple-negative breast cancer cell lines, MDA-MB-231 and BT-549, accompanied by the decrease of cyclin A2, cyclin B1, c-myc, and N-cadherin and the increase of E-cadherin. Collectively, these results indicate that C6orf106 may promote tumor progression in the invasive breast cancer, particularly in triple-negative breast cancer, and C6orf106 might serve as a novel therapeutic target of breast cancer, especially for triple-negative breast cancer.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A novel biomarker C6orf106 promotes the malignant progression of breast cancer

Jiang

Zhang

et al. 2015

Tumor Biol.

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“…For instance, GIT2-deficient mice exhibit elevated susceptibility to colon damage in two models of colitis and after peritoneal infection with E. coli (Wei et al, 2014). GIT2 interacts with and regulates the NFκB signaling pathway (Wang et al, 2011), and loss of GIT2 augments the signaling of the Toll-like receptor TLR4 to NFκB by facilitating deubiquitination of the E3 ligase TRAF6, which links TLR4 to NFκB (Wei et al, 2014). This leads to a dramatic increase in pro-inflammatory cytokines and amplified tissue damage.…”

Section: Functions In the Immune Systemmentioning

confidence: 99%

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

Weiyuan

Premont

2016

Journal of Cell Science

100

130

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The GIT proteins, GIT1 and GIT2, are GTPase-activating proteins (inactivators) for the ADP-ribosylation factor (Arf ) small GTP-binding proteins, and function to limit the activity of Arf proteins. The PIX proteins, α-PIX and β-PIX (also known as ARHGEF6 and ARHGEF7, respectively), are guanine nucleotide exchange factors (activators) for the Rho family small GTP-binding protein family members Rac1 and Cdc42. Through their multi-domain structures, GIT and PIX proteins can also function as signaling scaffolds by binding to numerous protein partners. Importantly, the constitutive association of GIT and PIX proteins into oligomeric GIT-PIX complexes allows these two proteins to function together as subunits of a larger structure that coordinates two distinct small GTP-binding protein pathways and serves as multivalent scaffold for the partners of both constituent subunits. Studies have revealed the involvement of GIT and PIX proteins, and of the GIT-PIX complex, in numerous fundamental cellular processes through a wide variety of mechanisms, pathways and signaling partners. In this Commentary, we discuss recent findings in key physiological systems that exemplify current understanding of the function of this important regulatory complex. Further, we draw attention to gaps in crucial information that remain to be filled to allow a better understanding of the many roles of the GIT-PIX complex in health and disease.

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“…The cross and capture system was specifically developed to identify and confirm yeast PPIs detected by other methods, including Y2H (Suter et al 2007;Suter 2012), and has successfully recapitulated interactions previously detected by Y2H (Suter et al 2007). Furthermore, similar coimmunoprecipitation assays have been used to validate Y2H data sets (Wang et al 2011;Hegele et al 2012). …”

Section: Validation Of the High-confidence Interactomementioning

confidence: 99%

A protein interaction map of the LSU processome

et al. 2015

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Maturation of the large ribosomal subunit (LSU) in eukaryotes is a complex and highly coordinated process that requires the concerted action of a large, dynamic, ribonucleoprotein complex, the LSU processome. While we know that >80 ribosome biogenesis factors are required throughout the course of LSU assembly, little is known about how these factors interact with each other within the LSU processome. To interrogate its organization and architecture, we took a systems biology approach and performed a semi-high-throughput, array-based, directed yeast two-hybrid assay. Assaying 4800 protein-protein interactions, we identified 232 high-confidence, binary-interacting protein pairs, representing a fourfold increase from current knowledge. The resulting LSU processome interactome map has enhanced our understanding of the organization and function of the biogenesis factors within the LSU processome, revealing both novel and previously identified subcomplexes and hub proteins, including Nop4.[Keywords: LSU processome; RNA; ribosome; yeast two-hybrid] Supplemental material is available for this article. Eukaryotic ribosomes are complex cellular machines that are comprised of four different ribosomal RNAs (rRNAs) and >70 ribosomal proteins (r-proteins) (Woolford and Baserga 2013). Ribosome assembly begins in the nucleolus with the transcription of the polycistronic pre-rRNA, termed the 35S in Saccharomyces cerevisiae, by RNA polymerase I. The 35S pre-rRNA undergoes numerous cleavage and modification steps to generate the mature 18S, 5.8S, and 25S rRNAs that are assembled with the r-proteins to form the small and large ribosomal subunits. Accurate and efficient production of ribosomes requires the coordinated activity of >150 biogenesis factors, including a number of proteins with enzymatic activity (Fatica and Tollervey 2002; Fromont-Racine et al.

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Toward an understanding of the protein interaction network of the human liver

Cited by 27 publications

References 0 publications

A novel biomarker C6orf106 promotes the malignant progression of breast cancer

A novel biomarker C6orf106 promotes the malignant progression of breast cancer

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

A protein interaction map of the LSU processome

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