Fig. 7: CDK6 phosphorylated human AMPKα and CHREBP directly.
From: CDK6 inhibits de novo lipogenesis in white adipose tissues but not in the liver
a Schematic depiction of phosphorylated sites on CHREBP, which contain a N-terminal domain (1-251), a proline-rich domain, and a DNA binding domain bHLH/ZIP. The N-terminal contains two nuclear export signals (NES1 and NES2) (1-95), a nuclear localization signal (NLS, 158-190), and domains named glucose-sensing module (GSM 1-251) critical for glucose regulation including low glucose inhibitory domain (LID) and a glucose-response activation conserved element (GRACE). The numbers above the schematic diagram indicated the phosphorylation occurred on serine (S)/threonine (T) residues. Non-CDK6-specific phosphorylation of S196, S602, and S618 were indicated by dotted lines. b, c Schematic depiction of phosphorylated sites on AMPKα1 b and AMPKα2 c, respectively. AMPKα contains a kinase catalytic domain (KCD, 1-314 for α1, 1-312 for α2), an auto inhibitory domain (AID) (313/315-335), and a β/γ binding domain (471-548/552). CDK6-specific phosphorylation sites were indicated by amino acid residue numbers above the schematic diagrams. Thr-172 was highlighted in red.
