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Junbao Yang, Zhiwei Zhang, Yingying Zhang, Xulei Zheng, Yilu Lu, Dachang Tao, Yunqiang Liu, Yongxin Ma
The core circadian gene CLOCK plays an important role in regulating male reproduction. However, the underlying mechanism still remains unclear. In the present study, we executed yeast two-hybrid screening using cDNA fragment of CLOCK PAS A domain as bait, and identified RANBP9 as a novel protein interacting with CLOCK. The interaction between CLOCK and RANBP9 was further validated by in vivo and in vitro assays. Previous studies have confirmed that SF3B3 was a RANBP9 interacting protein. Subsequently, our study also found that CLOCK and SF3B3 can interact with each other by co-immunoprecipitation in mouse testis...
February 5, 2018: Gene
Jung A Woo, Tian Liu, Xingyu Zhao, Courtney Trotter, Ksenia Yrigoin, Sara Cazzaro, Emilio De Narvaez, Hirah Khan, Richard Witas, Anusha Bukhari, Kamal Makati, Xinming Wang, Chad Dickey, David E Kang
Accumulation of amyloid β (Aβ) and tau represent the two major pathological hallmarks of Alzheimer's disease (AD). Despite the critical importance of Aβ accumulation as an early event in AD pathogenesis, multiple lines of evidence indicate that tau is required to mediate Aβ-induced neurotoxic signals in neurons. We have previously shown that the scaffolding protein Ran-binding protein 9 (RanBP9), which is highly elevated in brains of AD and AD mouse models, both enhances Aβ production and mediates Aβ-induced neurotoxicity...
October 15, 2017: Human Molecular Genetics
Zehang Zhao, Shan Cheng, Catherine Zabkiewicz, Jinfeng Chen, Lijiang Zhang, Lin Ye, Wen G Jiang
BACKGROUND/AIM: Ran binding protein microtubule-organizing centre (RanBPM), also known as RanBP9, is a scaffold protein conserved through evolution. We investigated the role of RanBPM in human lung cancer. MATERIALS AND METHODS: Transcripts of RanBPM were determined in 56 human lung cancers along with paired normal lung tissues using real-time PCR. Association with prognosis was analyzed by online Kaplan-Meier survival analysis. In vitro lung cancer cell functional assays examined the impact of RanBPM-knockdown on cellular growth and invasion...
August 2017: Anticancer Research
Louisa M Salemi, Matthew E R Maitland, Christina J McTavish, Caroline Schild-Poulter
RanBPM (Ran-binding protein M, also called RanBP9) is an evolutionarily conserved, ubiquitous protein which localizes to both nucleus and cytoplasm. RanBPM has been implicated in the regulation of a number of signalling pathways to regulate several cellular processes such as apoptosis, cell adhesion, migration as well as transcription, and plays a critical role during development. In addition, RanBPM has been shown to regulate pathways implicated in cancer and Alzheimer's disease, implying that RanBPM has important functions in both normal and pathological development...
June 2017: Open Biology
Kyeong-Won Yoo, Maivannan Thiruvarangan, Yun-Mi Jeong, Mi-Sun Lee, Sateesh Maddirevula, Myungchull Rhee, Young-Ki Bae, Hyung-Goo Kim, Cheol-Hee Kim
Ran-binding protein family member, RanBP9 has been reported in various basic cellular mechanisms and neuropathological conditions including schizophrenia. Previous studies have reported that RanBP9 is highly expressed in the mammalian brain and retina; however, the role of RanBP9 in retinal development is largely unknown. Here, we present the novel and regulatory roles of RanBP9 in retinal development of a vertebrate animal model, zebrafish. Zebrafish embryos exhibited abundant expression of ranbp9 in developing brain tissues as well as in the developing retina...
April 2017: Molecules and Cells
Huanzi Dai, Yang-Fan Lv, Guang-Ning Yan, Gang Meng, Xi Zhang, Qiao-Nan Guo
Suppression of anoikis is a prerequisite for tumor cell metastasis, which is correlated with chemoresistance and poor prognosis. We characterized a novel interaction between RanBP9 SPRY domain and TSSC3 PH domain by which RanBP9/TSSC3 complex exerts transcription and post-translation regulation in osteosarcoma. RanBP9/TSSC3 complex was inversely correlated with a highly anoikis-resistant phenotype in osteosarcoma cells and metastasis in human osteosarcoma. RanBP9 cooperated with TSSC3 to inhibit anchorage-independent growth and to promote anoikis in vitro and suppress lung metastasis in vivo...
December 29, 2016: Cell Death & Disease
Ore Francis, Genevieve E Baker, Paul R Race, Josephine C Adams
The mammalian muskelin/RanBP9/C-terminal to LisH (CTLH) complex and the Saccharomyces cerevisiae glucose-induced degradation (GID) complex are large, multi-protein complexes that each contain a RING E3 ubiquitin ligase. The yeast GID complex acts to degrade a key enzyme of gluconeogenesis, fructose 1,6-bisphosphatase, under conditions of abundant fermentable carbon sources. However, the assembly and functions of the mammalian complex remain poorly understood. A striking feature of these complexes is the presence of multiple proteins that contain contiguous lissencephaly-1 homology (LisH), CTLH and C-terminal CT11-RanBP9 (CRA) domains...
February 28, 2017: Bioscience Reports
Clara Bodelon, Hannah Oh, Nilanjan Chatterjee, Montserrat Garcia-Closas, Maya Palakal, Mark E Sherman, Ruth M Pfeiffer, Berta Geller, Pamela Vacek, Donald L Weaver, Rachael Chicoine, Daphne Papathomas, Jackie Xiang, Deesha A Patel, Zeina G Khodr, Laura Linville, Susan E Clare, Daniel W Visscher, Carolyn Mies, Stephen M Hewitt, Louise A Brinton, Anna Maria V Storniolo, Chunyan He, Stephen J Chanock, Gretchen L Gierach, Jonine D Figueroa
Terminal duct lobular units (TDLUs) are the predominant source of future breast cancers, and lack of TDLU involution (higher TDLU counts, higher acini count per TDLU and the product of the two) is a breast cancer risk factor. Numerous breast cancer susceptibility single nucleotide polymorphisms (SNPs) have been identified, but whether they are associated with TDLU involution is unknown. In a pooled analysis of 872 women from two studies, we investigated 62 established breast cancer SNPs and relationships with TDLU involution...
February 15, 2017: International Journal of Cancer. Journal International du Cancer
Sandrine Puverel, Erkan Kiris, Satyendra Singh, Kimberly D Klarmann, Vincenzo Coppola, Jonathan R Keller, Lino Tessarollo
c-Kit is a tyrosine kinase receptor important for gametogenesis, hematopoiesis, melanogenesis and mast cell biology. Dysregulation of c-Kit function is oncogenic and its expression in the stem cell niche of a number of tissues has underlined its relevance for regenerative medicine and hematopoietic stem cell biology. Yet, very little is known about the mechanisms that control c-Kit protein levels. Here we show that the RanBPM/RanBP9 scaffold protein binds to c-Kit and is necessary for normal c-Kit protein expression in the mouse testis and subset lineages of the hematopoietic system...
December 20, 2016: Oncotarget
L L Zhu, C H Wang, H P Yang, W H Shu
This study was carried out to investigate the expression changes of RanBP9 in tissue specimens and osteosarcoma cell strains and preliminarily explore its mechanism in osteosarcoma, so as to provide a theoretical foundation for follow-up experiments. The expression of RanBP9 in human osteosarcoma tissue specimens was detected by immunohistochemistry and the expression of RanBP9 messenger ribose nucleic acid (mRNA) in osteosarcoma cell strains was detected in real-time with polymerase chain reaction (PCR), and finally the expression of RanBP9 protein in osteosarcoma cell strains was detected by immunofluorescent staining and Western blot...
January 2016: Journal of Biological Regulators and Homeostatic Agents
Dario Palmieri, Mario Scarpa, Anna Tessari, Rexhep Uka, Foued Amari, Cindy Lee, Timothy Richmond, Claudia Foray, Tyler Sheetz, Ashley Braddom, Christin E Burd, Jeffrey D Parvin, Thomas Ludwig, Carlo M Croce, Vincenzo Coppola
Ran Binding Protein 9 (RanBP9, also known as RanBPM) is an evolutionary conserved scaffold protein present both in the nucleus and the cytoplasm of cells whose biological functions remain elusive. We show that active ATM phosphorylates RanBP9 on at least two different residues (S181 and S603). In response to IR, RanBP9 rapidly accumulates into the nucleus of lung cancer cells, but this nuclear accumulation is prevented by ATM inhibition. RanBP9 stable silencing in three different lung cancer cell lines significantly affects the DNA Damage Response (DDR), resulting in delayed activation of key components of the cellular response to IR such as ATM itself, Chk2, γH2AX, and p53...
April 5, 2016: Oncotarget
J Xie, R Gizatullin, V Vukojevic, R Leopardi
PURPOSE: Our previous study suggested that the coiled coil domain-containing 55 gene (CCDC55), also named as NSRP1 (nuclear speckle splicing regulatory protein 1 (NSRP1)), was encompassed in a haplotype block spanning over the serotonin transporter (5-HTT) gene in patients with schizophrenia (SCZ). However, the neurobiological function of CCDC55 gene remains unknown. This study aims to uncover the potential role of CCDC55 in SCZ-associated molecular pathways. EXPERIMENTAL DESIGN: Using molecular cloning, sequencing and immune blotting to identify basic properties, yeast two-hybrid screening and glutathione S-transferase (GST) pull-down assay to test protein-protein interaction, and confocal laser scanning microscopy (CSLM) to show intracellular interaction of proteins...
December 3, 2015: Neuroscience
A Rao, J Net, K Brandt, E Huang, J Freymann, E Burnside, J Kirby, E Morris, E Bonaccio, M Giger, C Jaffe, M Ganott, E Sutton, H Le-Petross, M Zuley, B Dogan, G Whitman
PURPOSE: To determine associations between radiologist-annotated MRI features and genomic measurements in breast invasive carcinoma (BRCA) from the Cancer Genome Atlas (TCGA). METHODS: 98 TCGA patients with BRCA were assessed by a panel of radiologists (TCGA Breast Phenotype Research Group) based on a variety of mass and non-mass features according to the Breast Imaging Reporting and Data System (BI-RADS). Batch corrected gene expression data was obtained from the TCGA Data Portal...
June 2015: Medical Physics
J A Woo, T Boggess, C Uhlar, X Wang, H Khan, G Cappos, A Joly-Amado, E De Narvaez, S Majid, L S Minamide, J R Bamburg, D Morgan, E Weeber, D E Kang
Molecular pathways underlying the neurotoxicity and production of amyloid β protein (Aβ) represent potentially promising therapeutic targets for Alzheimer's disease (AD). We recently found that overexpression of the scaffolding protein RanBP9 increases Aβ production in cell lines and in transgenic mice while promoting cofilin activation and mitochondrial dysfunction. Translocation of cofilin to mitochondria and induction of cofilin-actin pathology require the activation/dephosphorylation of cofilin by Slingshot homolog 1 (SSH1) and cysteine oxidation of cofilin...
2015: Cell Death & Disease
Ruizhi Wang, Hongjie Wang, Ivan Carrera, Shaohua Xu, Madepalli K Lakshmana
Brain accumulation of neurotoxic amyloid β (Aβ) peptide because of increased processing of amyloid precursor protein (APP), resulting in loss of synapses and neurodegeneration, is central to the pathogenesis of Alzheimer disease (AD). Therefore, the identification of molecules that regulate Aβ generation and those that cause synaptic damage is crucial for future therapeutic approaches for AD. We demonstrated previously that COPS5 regulates Aβ generation in neuronal cell lines in a RanBP9-dependent manner...
April 3, 2015: Journal of Biological Chemistry
Louisa M Salemi, Sandra O Loureiro, Caroline Schild-Poulter
RanBPM/RanBP9 is a ubiquitous, nucleocytoplasmic protein that is part of an evolutionary conserved E3 ubiquitin ligase complex whose function and targets in mammals are still unknown. RanBPM itself has been implicated in various cellular processes that involve both nuclear and cytoplasmic functions. However, to date, little is known about how RanBPM subcellular localization is regulated. We have conducted a systematic analysis of RanBPM regions that control its subcellular localization using RanBPM shRNA cells to examine ectopic RanBPM mutant subcellular localization without interference from the endogenously expressed protein...
2015: PloS One
Joon Seol Bae, Jason Yongha Kim, Byung-Lae Park, Hyun Sub Cheong, Jeong-Hyun Kim, Suhg Namgoong, Ji-On Kim, Chul Soo Park, Bong-Jo Kim, Cheol-Soon Lee, Migyung Lee, Woo Hyuk Choi, Tae-Min Shin, Jaeuk Hwang, Hyoung Doo Shin, Sung-Il Woo
Schizophrenia is a serious mental disorder that is affected by genetic and environmental factors. As the disease has a high heritability rate, genetic studies identifying candidate genes for schizophrenia have been conducted in various populations. The gene for human Ran‑binding protein 9 (RANBP9) is a newly discovered candidate gene for schizophrenia. As RANBP9 is a small guanosine‑5'‑triphosphate‑binding protein that interacts with the disrupted in schizophrenia 1 protein, it is considered to be an important molecule in the pathogenesis of schizophrenia...
April 2015: Molecular Medicine Reports
Jianqiang Bao, Chong Tang, Jiachen Li, Ying Zhang, Bhupal P Bhetwal, Huili Zheng, Wei Yan
As a member of the large Ran-binding protein family, Ran-binding protein 9 (RANBP9) has been suggested to play a critical role in diverse cellular functions in somatic cell lineages in vitro, and this is further supported by the neonatal lethality phenotype in Ranbp9 global knockout mice. However, the exact molecular actions of RANBP9 remain largely unknown. By inactivation of Ranbp9 specifically in testicular somatic and spermatogenic cells, we discovered that Ranbp9 was dispensable for Sertoli cell development and functions, but critical for male germ cell development and male fertility...
December 2014: PLoS Genetics
Sara C Domingues, Uwe Konietzko, Ana Gabriela Henriques, Sandra Rebelo, Margarida Fardilha, Hideo Nishitani, Roger M Nitsch, Edgar F da Cruz E Silva, Odete A B da Cruz E Silva
Proteolytic processing of the amyloid-β protein precursor (AβPP) occurs via alternative pathways, culminating with the production of the AβPP intracellular domain (AICD). AICD can translocate to the nucleus and regulate transcription, but its activity is modulated by interactions with other proteins. In the nucleus, AICD, FE65, and Tip60 associate into AFT complexes, which are targeted to nuclear spots which correspond to transcription factories. Here we report that RanBP9 interacts with the cytoplasmic domain of AβPP, through the NPXY internalization motif...
2014: Journal of Alzheimer's Disease: JAD
Ruizhi Wang, Juan Pablo Palavicini, Hongjie Wang, Panchanan Maiti, Elisabetta Bianchi, Shaohua Xu, B N Lloyd, Ken Dawson-Scully, David E Kang, Madepalli K Lakshmana
We previously demonstrated that RanBP9 overexpression increased Aβ generation and amyloid plaque burden, subsequently leading to robust reductions in the levels of several synaptic proteins as well as deficits in the learning and memory skills in a mouse model of Alzheimer's disease (AD). In the present study, we found striking reduction of spinophilin-immunoreactive puncta (52%, p<0.001) and spinophilin area (62.5%, p<0.001) in the primary cortical neurons derived from RanBP9 transgenic mice (RanBP9-Tg) compared to wild-type (WT) neurons...
September 2014: Neurobiology of Disease
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