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Orthologous residues
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NDR1 (human): S281‑p, NDR1 (mouse): S281‑p
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Characterization
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Methods used to characterize site in vivo:
microscopy-colocalization with upstream kinase, phospho-antibody, western blotting
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Disease tissue studied:
bone cancer
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Relevant cell lines - cell types - tissues:
COS (fibroblast), U2OS (bone cell)
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Cellular systems studied:
cell lines
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Species studied:
monkey
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Downstream Regulation
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Effect of modification (function):
enzymatic activity, induced, intracellular localization, phosphorylation
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Modification regulates interactions with:
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Interacting molecule
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Interacting domains
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Effect
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Consequences (function)
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Consequences (process)
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Detection assays
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MOBP (human)
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Induces
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co-immunoprecipitation
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Comments:
Myristoylated palmitylated NDR1 is membrane targeted and constitutively active (mp-HA-NDR1). When hMOB1A was coexpressed T444, and S281 phosphorylation were greatly increased in wild-type. Association with hMOB1A induces autophosphorylation of NDR1 on S281. A chimera of PKB and and the C1 domain of PKCa fused to hMOB1A recruited this chimera protein to the membrane after TPA treatment. TPA induction further induced the phosphorylation of NDR1 S281 and T444. A NDR1 mutant deficient in hMOB1A binding did not show an increase in phosphorylation.
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