PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM SHORT), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
findings advance our understanding of how phosphorylation of lipin 1beta phosphatidate phosphatase regulates its interaction with 14-3-3beta protein and intracellular localization and uncover a mechanism by which CKII regulates cellular physiology.
Data identified three classes of 14-3-3 targets that all have two binding sites but displayed synergistic interaction between converging signalling pathways for different ranges of parameter values.
KCNK3 potassium channels are shown to bear two cytoplasmic trafficking motifs: an N-terminal dibasic site that binds beta-COP to hold channels in ER and a C-terminal "release" site that binds the ubiquitous intracellular regulator 14-3-3beta
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