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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Chromosome 14 open reading frame 129

GSKIP, GSK3beta interaction protein
Top mentioned proteins: AML1, ACID, Axin, Utrophin, TCF
Papers on GSKIP
The A-kinase Anchoring Protein GSKIP Regulates GSK3β Activity and Controls Palatal Shelf Fusion in Mice.
Klussmann et al., Berlin, Germany. In J Biol Chem, Feb 2016
A member of this family is glycogen synthase kinase 3β (GSK3β) interaction protein (GSKIP).
Germline duplication of ATG2B and GSKIP predisposes to familial myeloid malignancies.
Plo et al., Villejuif, France. In Nat Genet, Oct 2015
Using induced pluripotent stem cells and primary cells, we demonstrate that overexpression of ATG2B and GSKIP enhances hematopoietic progenitor differentiation, including of megakaryocytes, by increasing progenitor sensitivity to thrombopoietin (TPO).
GSKIP- and GSK3-mediated anchoring strengthens cAMP/PKA/Drp1 axis signaling in the regulation of mitochondrial elongation.
Hong et al., Kao-hsiung, Taiwan. In Biochim Biophys Acta, Aug 2015
GSK3β binding of GSKIP affects neurite outgrowth, but the physiological significance of PKA binding to GSKIP remains to be determined.
Prediction of the binding mode between GSK3β and a peptide derived from GSKIP using molecular dynamics simulation.
Yang et al., Kao-hsiung, Taiwan. In Biopolymers, 2011
analysis of the GSK3beta-GSKIPtide complex structure and the X-ray crystal structures of GSK3beta-FRATide and GSK3beta-AxinGID complexes suggests that the hydroxyl group of Y288 is crucial to maintaining a hydrogen bond network in GSK3beta-FRATide
Involvement of the residues of GSKIP, AxinGID, and FRATtide in their binding with GSK3beta to unravel a novel C-terminal scaffold-binding region.
Hong et al., Kao-hsiung, Taiwan. In Mol Cell Biochem, 2010
In order to explore the mode that involved the binding of GSKIP to GSK3beta and compare it with that of AxinGID and FRATtide, we pinpointed the binding sites of GSKIP to GSK3beta through the single-point mutation of four corresponding sites within GSK3beta (residues 260-300) as scaffold-binding region I (designated SBR-I(260-300)).
Glycogen synthase kinase 3beta interaction protein functions as an A-kinase anchoring protein.
Klussmann et al., Berlin, Germany. In J Biol Chem, 2010
Our bioinformatics and peptide array screening approaches based on this signature motif identified GSKIP (glycogen synthase kinase 3beta interaction protein) as an AKAP.
GSKIP, an inhibitor of GSK3beta, mediates the N-cadherin/beta-catenin pool in the differentiation of SH-SY5Y cells.
Hong et al., Kao-hsiung, Taiwan. In J Cell Biochem, 2010
Our previous study has shown a novel GSK3beta interaction protein (GSKIP) able to negatively regulate GSK3beta in Wnt signaling pathway.
GSKIP is homologous to the Axin GSK3beta interaction domain and functions as a negative regulator of GSK3beta.
Hong et al., Kao-hsiung, Taiwan. In Biochemistry, 2006
GSKIP is a naturally occurring protein that is homologous with the GSK3beta interaction domain of Axin and is able to negatively regulate GSK3beta of the Wnt signaling pathway.
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