Energetic Determinants of Internal Motif Recognition by PDZ Domains

Biochemistry ◽  
2001 ◽  
Vol 40 (20) ◽  
pp. 5921-5930 ◽  
Author(s):  
Baruch Z. Harris ◽  
Brian J. Hillier ◽  
Wendell A. Lim
Keyword(s):  
Pdz Domains ◽  
Motif Recognition ◽  
Internal Motif

scholarly journals ZO-3, a Novel Member of the MAGUK Protein Family Found at the Tight Junction, Interacts with ZO-1 and Occludin

1998 ◽  
Vol 141 (1) ◽  
pp. 199-208 ◽  
Author(s):  
Julie Haskins ◽  
Lijie Gu ◽  
Erika S. Wittchen ◽  
Jennifer Hibbard ◽  
Bruce R. Stevenson
Keyword(s):  
Amino Acid ◽  
Tight Junction ◽  
Molecular Mass ◽  
Mdck Cells ◽  
Cdna Libraries ◽  
Pdz Domains ◽  
Large Tumor ◽  
Junction Protein ◽  
Discs Large

A 130-kD protein that coimmunoprecipitates with the tight junction protein ZO-1 was bulk purified from Madin-Darby canine kidney (MDCK) cells and subjected to partial endopeptidase digestion and amino acid sequencing. A resulting 19–amino acid sequence provided the basis for screening canine cDNA libraries. Five overlapping clones contained a single open reading frame of 2,694 bp coding for a protein of 898 amino acids with a predicted molecular mass of 98,414 daltons. Sequence analysis showed that this protein contains three PSD-95/SAP90, discs-large, ZO-1 (PDZ) domains, a src homology (SH3) domain, and a region similar to guanylate kinase, making it homologous to ZO-1, ZO-2, the discs large tumor suppressor gene product of Drosophila, and other members of the MAGUK family of proteins. Like ZO-1 and ZO-2, the novel protein contains a COOH-terminal acidic domain and a basic region between the first and second PDZ domains. Unlike ZO-1 and ZO-2, this protein displays a proline-rich region between PDZ2 and PDZ3 and apparently contains no alternatively spliced domain. MDCK cells stably transfected with an epitope-tagged construct expressed the exogenous polypeptide at an apparent molecular mass of ∼130 kD. Moreover, this protein colocalized with ZO-1 at tight junctions by immunofluorescence and immunoelectron microscopy. In vitro affinity analyses demonstrated that recombinant 130-kD protein directly interacts with ZO-1 and the cytoplasmic domain of occludin, but not with ZO-2. We propose that this protein be named ZO-3.

Structural Basis of PxxDY Motif Recognition in SH3 Binding

2008 ◽  
Vol 382 (1) ◽  
pp. 167-178 ◽  
Author(s):  
Olli Aitio ◽  
Maarit Hellman ◽  
Tapio Kesti ◽  
Iivari Kleino ◽  
Olga Samuilova ◽  
...  
Keyword(s):  
Structural Basis ◽  
Motif Recognition

scholarly journals The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex

Biochemistry ◽  
2015 ◽  
Vol 55 (1) ◽  
pp. 199-209 ◽  
Author(s):  
Sarah Clark ◽  
Afua Nyarko ◽  
Frank Löhr ◽  
P. Andrew Karplus ◽  
Elisar Barbar
Keyword(s):  
Motif Recognition

scholarly journals TRP and the PDZ Protein, Inad, Form the Core Complex Required for Retention of the Signalplex in Drosophila Photoreceptor Cells

2000 ◽  
Vol 150 (6) ◽  
pp. 1411-1422 ◽  
Author(s):  
Hong-Sheng Li ◽  
Craig Montell
Keyword(s):  
Transient Receptor Potential ◽  
Direct Interaction ◽  
Light Response ◽  
Receptor Potential ◽  
Photoreceptor Cells ◽  
Macromolecular Complex ◽  
Pdz Domains ◽  
The Core ◽  
Transient Receptor ◽  
Drosophila Photoreceptor

The light response in Drosophila photoreceptor cells is mediated by a series of proteins that assemble into a macromolecular complex referred to as the signalplex. The central player in the signalplex is inactivation no afterpotential D (INAD), a protein consisting of a tandem array of five PDZ domains. At least seven proteins bind INAD, including the transient receptor potential (TRP) channel, which depends on INAD for localization to the phototransducing organelle, the rhabdomere. However, the determinants required for localization of INAD are not known. In this work, we showed that INAD was required for retention rather than targeting of TRP to the rhabdomeres. In addition, we demonstrated that TRP bound to INAD through the COOH terminus, and this interaction was required for localization of INAD. Other proteins that depend on INAD for localization, phospholipase C and protein kinase C, also mislocalized. However, elimination of any other member of the signalplex had no impact on the spatial distribution of INAD. A direct interaction between TRP and INAD did not appear to have a role in the photoresponse independent of localization of multiple signaling components. Rather, the primary function of the TRP/ INAD complex is to form the core unit required for localization of the signalplex to the rhabdomeres.

scholarly journals Binding of PTEN to Specific PDZ Domains Contributes to PTEN Protein Stability and Phosphorylation by Microtubule-associated Serine/Threonine Kinases

2005 ◽  
Vol 280 (32) ◽  
pp. 28936-28943 ◽  
Author(s):  
Miguel Valiente ◽  
Amparo Andrés-Pons ◽  
Beatriz Gomar ◽  
Josema Torres ◽  
Anabel Gil ◽  
...  
Keyword(s):  
Protein Stability ◽  
Pdz Domains ◽  
Pten Protein ◽  
Threonine Kinases

scholarly journals PDZ Domains and Their Ligands

2004 ◽  
Vol 11 (4) ◽  
pp. 423-425 ◽  
Author(s):  
Brian K Kay ◽  
John W Kehoe
Keyword(s):  
Pdz Domains
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