scholarly journals Intramolecular Interactions Between the Src Homology 3 Guanylate Kinase Domains of Discs Large Regulate Its Function in Asymmetric Cell Division

2009 ◽  
Vol 284 (19) ◽  
pp. 12924-12932 ◽  
Author(s):  
Rhonda A. Newman ◽  
Kenneth E. Prehoda
Keyword(s):  
Cell Division ◽  
Asymmetric Cell Division ◽  
Intramolecular Interactions ◽  
Guanylate Kinase ◽  
Src Homology 3 ◽  
Discs Large ◽  
Src Homology

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 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 Conserved Discs-large Binding Partner Banderuola Regulates Asymmetric Cell Division in Drosophila

2014 ◽  
Vol 24 (16) ◽  
pp. 1811-1825 ◽  
Author(s):  
Federico Mauri ◽  
Ilka Reichardt ◽  
Jennifer L. Mummery-Widmer ◽  
Masakazu Yamazaki ◽  
Juergen A. Knoblich
Keyword(s):  
Cell Division ◽  
Asymmetric Cell Division ◽  
Binding Partner ◽  
Discs Large

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
Sign in / Sign up

Export Citation Format

Share Document