ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
MOB1 binds differently to the NDR2 and LATS1 kinases.MOB1 interaction with Hippo and MST protein is not essential for development and tissue growth control.
validated the functional importance of an identified interaction network by characterizing a distinct novel interaction between PTPN5 and Mob1a., Phosphorylation
In this study we investigated the mechanisms behind the recruitment of MST1 and MST2 kinases to MOB1 which facilitate signal transmission in the Hippo pathway by bringing the MST1 and MST2 kinases in close vicinity to their substrates the LATS family kinases.
Through a comprehensive set of biochemical biophysical mutational and structural studies we quantitatively assess how phosphorylation of MOB1A regulates its interaction with both MST kinases and LATS/NDR family kinases in vitro.
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