scholarly journals The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost

2002 ◽  
Vol 157 (1) ◽  
pp. 161-172 ◽  
Author(s):  
Michael H. Roh ◽  
Olga Makarova ◽  
Chia-Jen Liu ◽  
Shin ◽  
Seonok Lee ◽  
...  
Keyword(s):  
Tight Junctions ◽  
Protein Targeting ◽  
Pdz Domain ◽  
Guanylate Kinase ◽  
Src Homology 3 ◽  
Discs Large ◽  
Domain Of Unknown Function ◽  
Src Homology ◽  
Zona Occludens ◽  
Maguk Proteins

Membrane-associated guanylate kinase (Maguk) proteins are scaffold proteins that contain PSD-95–Discs Large–zona occludens-1 (PDZ), Src homology 3, and guanylate kinase domains. A subset of Maguk proteins, such as mLin-2 and protein associated with Lin-7 (Pals)1, also contain two L27 domains: an L27C domain that binds mLin-7 and an L27N domain of unknown function. Here, we demonstrate that the L27N domain targets Pals1 to tight junctions by binding to a PDZ domain protein, Pals1-associated tight junction (PATJ) protein, via a unique Maguk recruitment domain. PATJ is a homologue of Drosophila Discs Lost, a protein that is crucial for epithelial polarity and that exists in a complex with the apical polarity determinant, Crumbs. PATJ and a human Crumbs homologue, CRB1, colocalize with Pals1 to tight junctions, and CRB1 interacts with PATJ albeit indirectly via binding the Pals1 PDZ domain. In agreement, we find that a Drosophila homologue of Pals1 participates in identical interactions with Drosophila Crumbs and Discs Lost. This Drosophila Pals1 homologue has been demonstrated recently to represent Stardust, a crucial polarity gene in Drosophila. Thus, our data identifies a new multiprotein complex that appears to be evolutionarily conserved and likely plays an important role in protein targeting and cell polarity.

scholarly journals Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells

2002 ◽  
Vol 159 (2) ◽  
pp. 361-372 ◽  
Author(s):  
Sebastian Poliak ◽  
Sean Matlis ◽  
Christoph Ullmer ◽  
Steven S. Scherer ◽  
Elior Peles
Keyword(s):  
Tight Junction ◽  
Tight Junctions ◽  
Schwann Cells ◽  
Pdz Domain ◽  
Adaptor Protein ◽  
Dependent Manner ◽  
Guanylate Kinase ◽  
Pdz Proteins ◽  
Junction Protein ◽  
Zona Occludens

The apposed membranes of myelinating Schwann cells are joined by several types of junctional specializations known as autotypic or reflexive junctions. These include tight, gap, and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman, and mesaxons. The molecular components of autotypic tight junctions have not been established. Here we report that two homologues of Discs Lost–multi PDZ domain protein (MUPP)1, and Pals-associated tight junction protein (PATJ), are differentially localized in myelinating Schwann cells and associated with different claudins. PATJ is mainly found at the paranodal loops, where it colocalized with claudin-1. MUPP1 and claudin-5 colocalized in the incisures, and the COOH-terminal region of claudin-5 interacts with MUPP1 in a PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner. In developing nerves, claudin-5 and MUPP1 appear together in incisures during the first postnatal week, suggesting that they coassemble during myelination. Finally, we show that the incisures also contain four other PDZ proteins that are found in epithelial tight junctions, including three membrane-associated guanylate-kinase proteins (membrane-associated guanylate-kinase inverted-2, ZO-1, and ZO-2) and the adaptor protein Par-3. The presence of these different tight junction proteins in regions of noncompact myelin may be required to maintain the intricate cytoarchitecture of myelinating Schwann cells.

scholarly journals CARD11 and CARD14 Are Novel Caspase Recruitment Domain (CARD)/Membrane-associated Guanylate Kinase (MAGUK) Family Members that Interact with BCL10 and Activate NF-κB

2001 ◽  
Vol 276 (15) ◽  
pp. 11877-11882 ◽  
Author(s):  
John Bertin ◽  
Lin Wang ◽  
Yin Guo ◽  
Michael D. Jacobson ◽  
Jean-Luc Poyet ◽  
...  
Keyword(s):  
Pdz Domain ◽  
Family Members ◽  
Coiled Coil ◽  
Guanylate Kinase ◽  
Caspase Recruitment Domain ◽  
Src Homology 3 ◽  
Card Domain ◽  
Iκb Kinase ◽  
Src Homology 3 Domain ◽  
Src Homology

The caspase recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins into apoptosis and NF-κB signaling complexes. We report here that CARD protein 11 (CARD11) and CARD protein 14 (CARD14) are novel CARD-containing proteins that belong to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. CARD11 and CARD14 have homologous structures consisting of an N-terminal CARD domain, a central coiled-coil domain, and a C-terminal tripartite domain comprised of a PDZ domain, an Src homology 3 domain, and a GUK domain with homology to guanylate kinase. The CARD domains of both CARD11 and CARD14 associate specifically with the CARD domain of BCL10, a signaling protein that activates NF-κB through the IκB kinase complex in response to upstream stimuli. When expressed in cells, CARD11 and CARD14 activate NF-κB and induce the phosphorylation of BCL10. These findings suggest that CARD11 and CARD14 are novel MAGUK family members that function as upstream activators of BCL10 and NF-κB signaling.

scholarly journals The Gap Junction Protein Connexin32 Interacts with the Src Homology 3/Hook Domain of Discs Large Homolog 1

2007 ◽  
Vol 282 (13) ◽  
pp. 9789-9796 ◽  
Author(s):  
Heather S. Duffy ◽  
Ionela Iacobas ◽  
Kylie Hotchkiss ◽  
Bethany J. Hirst-Jensen ◽  
Alejandra Bosco ◽  
...  
Keyword(s):  
Gap Junction ◽  
Src Homology 3 ◽  
Junction Protein ◽  
Discs Large ◽  
Src Homology ◽  
Gap Junction Protein

scholarly journals The Src Homology 3 Domain Is Required for Junctional Adhesion Molecule Binding to the Third PDZ Domain of the Scaffolding Protein ZO-1

2011 ◽  
Vol 286 (50) ◽  
pp. 43352-43360 ◽  
Author(s):  
Julian Nomme ◽  
Alan S. Fanning ◽  
Michael Caffrey ◽  
Ming F. Lye ◽  
James M. Anderson ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Pdz Domain ◽  
Scaffolding Protein ◽  
Src Homology 3 ◽  
The Third ◽  
Src Homology 3 Domain ◽  
Src Homology

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

2010 ◽  
Vol 285 (18) ◽  
pp. 13907-13917 ◽  
Author(s):  
Ming F. Lye ◽  
Alan S. Fanning ◽  
Ying Su ◽  
James M. Anderson ◽  
Arnon Lavie
Keyword(s):  
Ligand Binding ◽  
Binding Sites ◽  
Guanylate Kinase ◽  
Src Homology 3 ◽  
Ligand Binding Sites ◽  
Src Homology

scholarly journals Functional dissection of the intramolecular Src homology 3-guanylate kinase domain coupling in voltage-gated Ca2+ channel β-subunits

FEBS Letters ◽  
2009 ◽  
Vol 583 (12) ◽  
pp. 1969-1975 ◽  
Author(s):  
Yu-hang Chen ◽  
Lin-ling He ◽  
Douglas R. Buchanan ◽  
Yun Zhang ◽  
Aileen Fitzmaurice ◽  
...  
Keyword(s):  
Kinase Domain ◽  
Guanylate Kinase ◽  
Voltage Gated ◽  
Src Homology 3 ◽  
Src Homology ◽  
Domain Coupling
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