Disease relevance of RANBP9

• In addition, transient overexpression of RanBPM in prostate cancer cell lines resulted in enhanced AR activity in a ligand-dependent fashion [1].
• CONCLUSIONS: These findings support the hypothesis that psoriasin may interact with RanBPM and this may influence both epithelial and stromal cells and thus contribute to breast tumor progression [2].
• RanBPM mRNA is also frequently expressed in invasive breast carcinomas (n = 64) and a higher psoriasin/RanBPM ratio is associated with both ER negative (p < 0.0001) and PR negative status (p < 0.001), and inflammatory cell infiltrates (p < 0.0001) within the tumor [2].
• Elevated levels of RanBP7 mRNA in colorectal carcinoma are associated with increased proliferation and are similar to the transcription pattern of the proto-oncogene c-myc [3].

High impact information on RANBP9

• The formation of microtubule asters was inhibited not only by anti- RanBPM antibodies, but also by nonhydrolyzable GTP-Ran [4].
• RanBPM cosedimented with the centrosomal fractions by sucrose- density gradient centrifugation [4].
• Anti-RanBPM antibodies revealed that RanBPM was localized within the centrosome throughout the cell cycle [4].
• RanBPM inhibited the kinase activity of Mirk/Dyrk1B and Dyrk1A [5].
• Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M [5].

Biological context of RANBP9

• Our findings suggest that Mirk plays a role in modulating cell migration through opposing the action of the Met signaling cascade adaptor protein RanBPM [5].
• Accordingly, in the present study, we screened the human cDNA library by the two-hybrid method using RanBPM cDNA as bait [6].
• To investigate the potential role of RanBPM in thyroid hormone action, transient transfections with luciferase reporter genes were performed in CV-1 cells [7].
• Furthermore, we performed competition assays using transient transfection of RanBPM and increasing amounts of RanBPM55 [7].
• This suggests that although the polyglutaminated region of RanBPM is not required for the binding to TRs, it is required for the stimulation of TR transactivation [7].

Anatomical context of RANBP9

• Here we have identified Ran-binding protein in the microtubule-organizing center (RanBPM) to be a novel AR-interacting protein by yeast two-hybrid assay and have confirmed this interaction by glutathione S-transferase- and His-tagged pull-down assays [1].
• Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells [8].
• Co-expression of RanBPM with p73alpha resulted in the nuclear translocation of RanBPM, and both proteins co-localized in cell nucleus as examined by indirect immunofluorescent staining [8].
• Knockdown of RanBP9 expression did not restore the differentiation program to Raf-expressing myoblasts [9].
• Endogenous CD39 and RanBPM are also found to be co-expressed and abundant in cell membranes of B-lymphocytes [10].

Associations of RANBP9 with chemical compounds

• The Mirk-RanBPM association was confirmed by glutathione S-transferase pull-down assays, co-immunoprecipitation studies, and in vivo cross-linking [5].
• These data demonstrate that RanBPM interacts with steroid receptors to selectively modify their activity [1].
• Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors [7].
• In conclusion, we have identified and characterised a novel interaction between RanBPM and the related receptor tyrosine kinases, Axl and Sky. This novel insight into the signalling interactions of Axl and Sky may shed further light on their suspected roles in tumourigenesis, inflammation as well as other cell proliferative diseases [11].
• Target peptides from Ran-binding protein M and myo-inositol monophosphatase, along with a new target from procaspase-3, are shown to interact with the protein on a surface comprised of alpha5 (EF3), alpha8 (EF4) and the EF2-EF3 and EF4-EF5 loops [12].

Physical interactions of RANBP9

• A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM [6].
• A carboxy- and an amino-terminal deletion of HIPK2 do not seem to be able to bind to RanBPM [13].
• Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy [14].
• RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer [2].
• The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM [15].

Regulatory relationships of RANBP9

• Glucocorticoid receptor activity was also enhanced when RanBPM was overexpressed, whereas estrogen receptor activity remained unchanged [1].
• We conclude that CD39 associations with RanBPM have the potential to regulate NTPDase catalytic activity [10].

Other interactions of RANBP9

• RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor [1].
• RanBPM was also found to interact in yeast with the Axl homologue, Sky/Tyro3 [11].
• HIPK2 associates with RanBPM [13].
• We suggest that the interaction between calbindin D(28K) and Ran-binding protein M may be important in calbindin D(28K) function [14].
• A recently found novel Ran-binding protein, RanBPM, however, is localized in the centrosome [16].

Analytical, diagnostic and therapeutic context of RANBP9

• Sequence analysis revealed that cDNA inserts of two colonies were highly homologous to a known human protein, RanBPM [17].
• RT-PCR analysis of RanBPM mRNA expression in cell lines (n = 13) shows that RanBPM is widely expressed in different cell types and that expression is higher in tumor than in normal breast epithelial cell lines [2].
• Bpml digestion of the resultant PCR products yields fragments as small as seven bases, which are then analyzed by electrospray ionization mass spectrometry [18].
• Images obtained by immunofluorescence and confocal scanning microscopy of CHO-K1 cells co-transfected with pEGFP-C1-hSMP-1 and pDsRed1-Nl-RanBPM revealed that RanBPM and hSMP-1 are distributed in discrete loci throughout the cytoplasm [19].

References