Nov 27, 2021 · GSK3 must be particularly adaptable for incorporating new substrates into its repertoire, and we discuss the distinct properties of GSK3 that may contribute to its capacity to fulfill its roles in multiple signaling pathways.

It contains a single PPPSPT motif, and phosphorylation of this motif by GSK3 and CKIα) promotes the ZBED3–AXIN interaction. CAPRIN2 and ZBED3 might modulate Wnt signaling via changes in their expression levels.

Mar 18, 2014 · We present crystal structures of GSK-3 bound to its phosphorylated N-terminus and to two of the phosphorylated LRP6 motifs. A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition.

GSK3β was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3β prefers prior phosphorylation of its substrates. We...

Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS (p), by recognizing and phosphorylating the first serine in the sequence motif SxxxS (P) (where S (p) represents a phosphoserine).

Glycogen synthase kinase-3 (GSK-3) is a constitutively active, ubiquitously expressed protein kinase that regulates multiple signaling pathways. In vitro kinase assays and genetic and pharmacological manipulations of GSK-3 have identified more than 100 putative GSK-3 substrates in diverse cell types.

This motif is subject to GSK-3 phosphorylation, promoting ER retention, while mutation of target serines and drug inhibition of GSK-3 activity coordinately induce both forward transport of the precursor and cleavage, resulting in nuclear import.

Background: Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS (p), by recognizing and phosphorylating the first serine in the sequence motif SxxxS (P) (where S (p) represents a phosphoserine).

Jan 1, 2017 · The activation domain starts with the DFG motif and ends with the APE motif. GSK-3’s structure most closely resembles mitogen-activated protein kinases (MAPKs). MAPKs require phosphorylation of two residues within their T-loop for activation. These residues include a tyrosine and a threonine.

We show that GSK-3beta binds to and phosphorylates Snail at two consensus motifs to dually regulate the function of this protein. Phosphorylation of the first motif regulates its beta-Trcp-mediated ubiquitination, whereas phosphorylation of …