High impact information on Ranbp9

• In the same assay, RanBPM also interacted with the beta(1) integrin cytoplasmic domain [1].
• We find that RanBPM is phosphorylated on serine residues; phosphorylation of RanBPM is increased by stress stimuli and decreased by treatment with the p38 kinase inhibitor SB203580 [1].
• Transfection of RanBPM synergizes with LFA-1-mediated adhesion in the transcriptional activation of an AP-1-dependent promoter, indicating that the two proteins interact functionally as well [1].
• We demonstrate that RanBPM is a peripheral membrane protein and that integrins and RanBPM interact in vitro and in vivo and co-localize at the cell membrane [1].
• On the cellular level, A704 cells, a human renal carcinoma cell line, transfected with RanBPM exhibit increased migration ability [2].

Biological context of Ranbp9

• Using the yeast two-hybrid system, we found that MVH interacts with mouse RanBPM, a Ran-GTP binding protein involved in microtubule nucleation [3].
• The interaction of MVH with RanBPM points to a functional relationship between translational regulation and the microtubule nucleation during meiosis [3].
• A yeast two-hybrid screen using the last 28 amino acids of the cytoplasmic domain of the neural cell adhesion molecule L1 identified RanBPM as an L1-interacting protein [4].

Anatomical context of Ranbp9

• RanBPM is predominantly expressed in the testis, especially in maturating spermatocytes [3].
• L1 antibody patching dramatically changes the subcellular localization of N-RanBPM in transfected COS cells [4].
• In brain tissue sections, RanBPM is highly expressed in the neurons of cerebral cortex and the cerebellar purkinje cells, in a pattern similar to that described for FMRP [5].

Associations of Ranbp9 with chemical compounds

• We demonstrate that RanBPM, which itself is not a guanine exchange protein, stimulates Ras activation by recruiting Sos [2].
• Our data suggest that RanBPM, functioning as an adaptor protein for the MET tyrosine kinase domain, can augment the HGF-MET signaling pathway and that RanBPM overexpression may cause constitutive activation of the Ras signaling pathway [2].
• Thus, full-sized RanBPM cDNA encodes a long stretch of proline and glutamine residues in the N-terminal region [6].
• Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex [6].

Physical interactions of Ranbp9

• RanBPM is a novel binding protein for p75NTR [7].

Other interactions of Ranbp9

• Mouse RanBPM is a partner gene to a germline specific RNA helicase, mouse vasa homolog protein [3].
• Using yeast two-hybrid system, we identified the Ran-binding protein (RanBPM) as an interactor with the intracytoplasmic domain of p75NTR (p75ICD) [7].

Analytical, diagnostic and therapeutic context of Ranbp9

• To characterize the mechanism, we searched for RanBPM-binding proteins by using a yeast two-hybrid method and isolated a cDNA encoding the ubiquitin-specific protease USP11 [8].
• Sequence analysis shows that RanBPM is a multi-domain protein [5].

References