A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling

RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors

“…There are several conserved domains including a proline-and glutamine-rich N-terminal segment thought to mediate formation of protein complexes (Nishitani et al, 2001), an SPRY (SP1a and ryanodine receptor) domain that is a protein interaction motif shared with the ryanodine receptor, and regions that share homology with Lis1 [Lissencephaly type-1-like homology and C-terminal to LisH (LisH-CTLH)], a dyneinregulating protein critical in neuronal migration (Wang et al, 2002). RanBPM has been demonstrated to localize primarily to the cytoplasmic face of the plasma membrane and to interact with integrin ␤ subunits and the hepatocyte growth factor receptor Met to modulate cellular morphology and motility (Wang et al, 2002(Wang et al, , 2004Denti et al, 2004).…”

Identification of RanBP 9/10 as Interacting Partners for Protein Kinase C (PKC) γ/δ and the D1Dopamine Receptor: Regulation of PKC-Mediated Receptor Phosphorylation

“…Although RanBP10 and RanBP9 do not seem to mediate the EtOH-induced attenuation of PKC␥ and PKC␦ kinase activities, they could function as important PKC scaffolding proteins. In fact, a role for RanBP10 and RanBP9 as scaffolding proteins has been well described previously (Wang et al, 2004;Haase et al, 2008;Talbot et al, 2009). In particular, both Ran10 and RanBP9 have been reported to associate with receptors expressed at the plasma membrane that include the MET tyrosine kinase receptor and the -opioid receptor, respectively (Wang et al, 2004;Talbot et al, 2009).…”

“…that is expressed in a variety of tissues including the brain (Wang et al, 2004;Haase et al, 2008;Schulze et al, 2008) and is known to interact with several proteins that include the protein Ran and the receptor protein tyrosine kinase for hepatocyte growth factor, MET (Wang et al, 2004). It is noteworthy that there is a closely related protein, RanBP9, that has high sequence similarity to RanBP10 (Wang et al, 2004) and has been found to associate with several GPCRs, including the -opioid receptor and the metabotropic glutamate receptors (mGluRs) mGluR2 and mGluR8, as well as with MET (Wang et al, 2004;Seebahn et al, 2008;Talbot et al, 2009). Figure 3 shows a structural comparison of RanBP9 and RanBP10 highlighting several conserved protein-protein interactions and functional domains such as dual-specific kinase splA and ryanodine receptor, lissencephaly type-1-like homology, Ran protein binding domain, and guanine nucleotide exchange factor domain (Schulze et al, 2008).…”

“…RanBP9 also associates with mGluR2 and mGluR8 in both HEK293 cells and the synaptic layers of the retina (Seebahn et al, 2008), although the role of RanBP9 in regu- lating glutamatergic signaling is currently unclear (Seebahn et al, 2008). Compared with RanBP9, there is little published information regarding RanBP10-dependent modulation of signaling; however, both RanBP10 and RanBP9 are described as scaffolding proteins for MET, a membranebound receptor tyrosine kinase for hepatocyte growth factor (Wang et al, 2004). Association of RanBP9 with MET increases recruitment of the protein SOS to MET and enhances ERK signaling.…”

Cellular Transcriptional Coactivator RanBP10 and Herpes Simplex Virus 1 ICP0 Interact and Synergistically Promote Viral Gene Expression and Replication

“…Among the putative ICP0-interacting cell proteins identified, we focused on RanBP10. RanBP10 was originally identified on the basis of its homology to RanBP9, a protein that binds a small Ras-like Ran GTPase involved in regulation of transport through nuclear pores (28,29), and is ubiquitously expressed in human tissues and expressed in various cell types in cell cultures (28,30). RanBP10 was reported to have multiple functions through its interaction with various proteins (30,31).…”