Molecular basis for the substrate specificity of plant guanine nucleotide exchange factors for ROP |
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| Authors: | Inka Fricke |
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| Affiliation: | Max Planck Institute of Molecular Physiology, Structural Biology Department, Otto Hahn Strasse 11, 44227 Dortmund, Germany |
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| Abstract: | Plant G proteins of the ROP/RAC family regulate cellular processes including cytoskeletal rearrangement in polar growth. Activation of the ROP molecular switch is triggered by guanine nucleotide exchange factors. Plant-specific RopGEFs are exclusively active on ROPs despite their high homology to animal Rho proteins. Based on a sequence comparison of ROPs vs. animal Rho proteins together with structural data on distinct ROPs, we identified unique substrate determinants of RopGEF specificity by mutational analysis: asparagine 68 next to switch II, arginine 76 of a putative phosphorylation motif and the Rho insert are essential for substrate recognition by RopGEFs. These data also provide first evidence for a function of the Rho insert in interactions with GEFs. |
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| Keywords: | At, Arabidopsis thaliana Cdc42, cell division cycle 42 cDNA, complementary DNA Dbl, diffuse B-cell lymphoma DH, Dbl homology G protein, guanine nucleotide binding protein GDI, guanine nucleotide dissociation inhibitor GEF, guanine nucleotide exchange factor GNP, GppNHp GST, glutathione-S-transferase HVR, hypervariable region IgG, immunoglobulin G P-loop, phosphate binding loop PCR, polymerase chain reaction PH, Pleckstrin homology PRONE, plant-specific ROP nucleotide exchanger Rac/RAC, Ras-related C3 botulinum toxin substrate Ras, rat sarcoma Rho, Ras homologue ROP, Rho of plants Tiam1, T-cell lymphoma invasion and metastasis 1 3D structure, three-dimensional structure |
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