Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho‐protein‐binding modules

@article{Zhu2011GuanylateKD,
  title={Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho‐protein‐binding modules},
  author={Jinwei Zhu and Yuan Shang and Caihao Xia and Wenning Wang and Wenyu Wen and Mingjie Zhang},
  journal={The EMBO Journal},
  year={2011},
  volume={30},
  url={https://api.semanticscholar.org/CorpusID:12993753}
}
The discovery of the phosphorylation‐dependent MAGUK GK/target interactions indicates that MAGUK scaffold‐mediated signalling complex organizations are dynamically regulated.
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106 Citations
Highly Influential Citations
8
Background Citations
43
Methods Citations
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Results Citations
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106 Citations

Phosphorylation-dependent recognition of diverse protein targets by the cryptic GK domain of MAGI MAGUKs

It is demonstrated that the truncated GK domain of MAGI2 interacts with its adjacent PDZ0 domain to form a structural supramodule capable of recognizing phosphoproteins, which expands the understanding of the target recognition rules of phosphoprotein binding modules.

Structure of an Enzyme-Derived Phosphoprotein Recognition Domain

The structure of the Dlg-Pins complex is determined to understand the dramatic transition from nucleotide kinase to phosphoprotein recognition domain and reveals that the region of the GKdom that once served as the GMP binding domain (GBD) has been co-opted for protein interaction.

An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B.

Structure and function of the guanylate kinase-like domain of the MAGUK family scaffold proteins

This review summarizes the structural basis governing cellular function of various members of the MAGUKs and focuses on recent discoveries of MAGUK GKs as specific phospho-protein interaction modules, and discusses functional implications and connections to human diseases of such regulated MAGuk GK/target interactions.

MAGUKs end a tale of promiscuity

Li et al. (3) prove that the clasp accounts for the high affinity and specificity of Crb binding to PALS1 and has immediate consequences for other MAGUKs, for example at synapses in the brain, because the authors propose that sequence variations within the clasp-loop are responsible for defining their specificity.

Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97).

Structure of the PSD-95/MAP1A complex reveals a unique target recognition mode of the MAGUK GK domain.

It is demonstrated that the MAP1A peptide may undergo a conformational transition upon binding to PSD-95 GK, which reveals the target recognition specificity and versatility of DLG GKs.

Characterizing the Binding Sites for GK Domain of DLG1 and DLG4 via Molecular Dynamics Simulation

Investigation into the interactions of DLG1 and DLG4 with their reported phosphor-peptides by molecular dynamics simulations showed thatDLG1/4 formed extensive interactions with phosphorylated ligands, including hydrophobic and hydrogen bonding interactions, which might be helpful for the better understanding of the structural and biological function of DLGs GK domain.

Mechanisms of MAGUK-mediated cellular junctional complex organization.

Involvement of SAP97 anchored multiprotein complexes in regulating cardiorenal signaling and trafficking networks.

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55 References

Functional Analysis of the Nucleotide Binding Domain of Membrane-associated Guanylate Kinases*

Surprisingly, and in contrast to previously published studies, GMP binding to the MAGUKs postsynaptic density-95 (PSD-95) and CASK is failed, indicating that MAGUK proteins have lost affinity for GMP but may have retained the guanylate kinase structure to accommodate a related regulatory ligand.

Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.

GKAP, a Novel Synaptic Protein That Interacts with the Guanylate Kinase-like Domain of the PSD-95/SAP90 Family of Channel Clustering Molecules

The isolation of a novel synaptic protein, termed GKAP for guanylate kinase-associated protein, that binds directly to the GK domain of the four known members of the mammalian PSD-95 family, shows a unique domain structure and appears to be a major constituent of the postsynaptic density.

Insights into Regulated Ligand Binding Sites from the Structure of ZO-1 Src Homology 3-Guanylate Kinase Module*

Insight is provided into the previously observed ability of the U6 region to regulate TJ assembly in vivo and the structural basis for the complex protein interactions of the MAGUK family is provided.

An Intramolecular Interaction between Src Homology 3 Domain and Guanylate Kinase-Like Domain Required for Channel Clustering by Postsynaptic Density-95/SAP90

A direct protein–protein interaction between the SH3 domain and the GK region in the PSD-95 family of MAGUKs is reported, suggesting that the intramolecular SH3–GK interaction may modulate the clustering activity of PSd-95.

Phosphoserine/threonine-binding domains.

Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions.

Diverse roles in tissue development, differentiation, and physiology are explained by recent biochemical and structural analyses of MAGUKs, which demonstrate their capacity to assemble well--efined--yet adaptable--protein complexes at cellular junctions.

Calcium Channel Function Regulated by the SH3-GK Module in β Subunits

Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

Membrane-associated guanylate kinase-like properties of beta-subunits required for modulation of voltage-dependent Ca2+ channels.

Findings reveal MAGUK-like properties in beta-subunits that are critical for alpha1-subunit modulation, revise current models ofalpha1-beta association, and predict new physiological dimensions of beta- subunit function.
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