title: The N-terminal region of the Neurospora NDR kinase COT1 regulates morphology via its interactions with MOB2A/B.
abstract: Nuclear Dbf2p-related (NDR) protein kinases are important for cell differentiation and polar morphogenesis in various organisms, yet some of their functions are still elusive. Dysfunction of the Neurospora crassa NDR kinase COT1 leads to cessation of tip extension and hyperbranching. NDR kinases require the physical interaction between the kinase's N-terminal region (NTR) and the MPS1-binding (MOB) proteins for their activity and functions. To study the interactions between COT1 and MOB2 proteins, we mutated several conserved residues and a novel phosphorylation site within the COT1 NTR. The phenotypes of these mutants suggest that the NTR is required for COT1 functions in regulating hyphal elongation and branching, asexual conidiation and germination. Interestingly, while both MOB2A and MOB2B promote proper hyphal growth, they have distinct COT1-dependent roles in regulation of macroconidiation. Immunoprecipitation experiments indicate physical association of COT1 with both MOB2A and MOB2B, simultaneously. Furthermore, the binding of the two MOB2 proteins to COT1 is mediated by different residues at the COT1 NTR, suggesting a hetero-trimer is formed. Thus, although MOB2A/B may have some overlapping functions in regulating hyphal tip extension, their function is not redundant and they are both required for proper fungal development.
authors: Department of Plant Pathology and Microbiology, The Otto Warburg Minerva Center for Agricultural Biotechnology, Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Rehovot, 76100, Israel.
authors: Carmit
authors: C
authors: Ziv
authors: Daria
authors: D
authors: Feldman
authors: Liran
authors: L
authors: Aharoni-Kats
authors: She
authors: S
authors: Chen
authors: Yi
authors: Y
authors: Liu
authors: Oded
authors: O
authors: Yarden
mesh_terms: D019943:Amino Acid Substitution; D001120:Arginine; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D025301:Hyphae / Q000378:metabolism; D009492:Neurospora crassa / Q000166:cytology / Q000254:growth & development / Q000502:physiology*; D010641:Phenotype; D010766:Phosphorylation; D017354:Point Mutation; D011485:Protein Binding; D060066:Protein Interaction Maps; D020033:Protein Isoforms; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D013172:Spores, Fungal / Q000502:physiology; D020798:Two-Hybrid System Techniques
chemical_list: D005656:Fungal Proteins; D020033:Protein Isoforms; D001120:Arginine; D017346:Protein Serine-Threonine Kinases
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