PMID: 18362890 RLIMS-P 3 Check other iTextMine results Issue Report
Title
| 1. | Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1. |
Abstract
| 2. | Mammalian nuclear Dbf2-related (NDR) kinases (LATS1 and 2, NDR1 and 2) play a role in cell proliferation, apoptosis and morphological changes. |
| 3. | These kinases are regulated by mammalian sterile 20-like kinases (MSTs) and Mps one binder (MOB) 1. |
| 4. | Okadaic acid (OA), which activates MST2, facilitates the complex formation of MOB1, MST2 and NDR1 in HEK293FT cells. |
| 5. | The in vitro biochemical study demonstrates the phosphorylation of MOB1 by MST2. |
| 6. | The phosphorylated MOB1 alone is capable to partially activate NDR1 in vitro, but MST2 is also required for the full activation. |
| 7. | The knockdown of MOB1 or MST2 abolishes the OA-induced NDR1 activation in HEK293FT cells. |
| 8. | Among MOB1 mutants, in which each serine or threonine residue is replaced with alanine, MOB1 T74A and T181A mutants fail to activate NDR1. |
| 9. | Thr74, but not Thr181, is phosphorylated by MST2 in vitro, although MOB1 is also phosphorylated by MST2 at other site(s). |
| 10. | The interaction of MOB1 T74A with NDR1 is barely enhanced by OA treatment. |
| 11. | These findings indicate that the phosphorylation of MOB1 at Thr74 by MST2 is essential to make a complex of MOB1, MST2 and NDR1, and to fully activate NDR1. |
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