Abstract:
:Downregulation of the LATS1 tumour suppressor protein kinase contributes to tumour formation in mammals and flies. Strikingly, the tumour suppressor activity depends on the interaction with Dmob (Drosphila Mps1-One binder) in Drosophila melanogaster. Recently, human LATS1 was reported to interact with human MOB1 (hMOB1), but the activation of LATS1 was not addressed. Here, we identified a highly conserved hMOB1-binding motif within LATS1's primary structure. While co-expression of LATS1 with hMOB1 did not elevate LATS1 kinase activity in mammalian cells, membrane-targeting of hMOB1 resulted in a significant increase of LATS1 activity. This stimulation was dependent on intact activation segment and hydrophobic motif phosphorylation sites, and was further found to occur a few minutes after membrane association. Therefore, we suggest a potential in vivo mechanism of LATS1 activation through rapid recruitment to the plasma membrane by hMOB1 followed by multi-site phosphorylation, thereby providing insight into the molecular regulation of the LATS tumour suppressor.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Hergovich A,Schmitz D,Hemmings BAdoi
10.1016/j.bbrc.2006.03.244subject
Has Abstractpub_date
2006-06-23 00:00:00pages
50-8issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)00793-5journal_volume
345pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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