Literature DB >> 11591811

Mechanism and role of PDZ domains in signaling complex assembly.

B Z Harris1, W A Lim.   

Abstract

PDZ domains are protein-protein recognition modules that play a central role in organizing diverse cell signaling assemblies. These domains specifically recognize short C-terminal peptide motifs, but can also recognize internal sequences that structurally mimic a terminus. PDZ domains can therefore be used in combination to bind an array of target proteins or to oligomerize into branched networks. Several PDZ-domain-containing proteins play an important role in the transport, localization and assembly of supramolecular signaling complexes. Examples of such PDZ-mediated assemblies exist in Drosophila photoreceptor cells and at mammalian synapses. The predominance of PDZ domains in metazoans indicates that this highly specialized scaffolding module probably evolved in response to the increased signaling needs of multicellular organisms.

Entities:  

Mesh:

Substances:

Year:  2001        PMID: 11591811     DOI: 10.1242/jcs.114.18.3219

Source DB:  PubMed          Journal:  J Cell Sci        ISSN: 0021-9533            Impact factor:   5.285


  256 in total

1.  Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs.

Authors:  Manabu Nakayama; Reiko Kikuno; Osamu Ohara
Journal:  Genome Res       Date:  2002-11       Impact factor: 9.043

2.  A conformational switch in the CRIB-PDZ module of Par-6.

Authors:  Dustin S Whitney; Francis C Peterson; Brian F Volkman
Journal:  Structure       Date:  2011-11-09       Impact factor: 5.006

3.  A protein-domain microarray identifies novel protein-protein interactions.

Authors:  Alexsandra Espejo; Jocelyn Côté; Andrzej Bednarek; Stephane Richard; Mark T Bedford
Journal:  Biochem J       Date:  2002-11-01       Impact factor: 3.857

4.  A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones.

Authors:  Yun Wang; Xinran Liu; Thomas Biederer; Thomas C Südhof
Journal:  Proc Natl Acad Sci U S A       Date:  2002-10-21       Impact factor: 11.205

5.  Suppression of integrin activation by the membrane-distal sequence of the integrin alphaIIb cytoplasmic tail.

Authors:  Jun Yamanouchi; Takaaki Hato; Tatsushiro Tamura; Shigeru Fujita
Journal:  Biochem J       Date:  2004-04-15       Impact factor: 3.857

6.  The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain.

Authors:  G Radziwill; R A Erdmann; U Margelisch; K Moelling
Journal:  Mol Cell Biol       Date:  2003-07       Impact factor: 4.272

7.  The scaffold protein PDZK1 undergoes a head-to-tail intramolecular association that negatively regulates its interaction with EBP50.

Authors:  David P LaLonde; Anthony Bretscher
Journal:  Biochemistry       Date:  2009-03-17       Impact factor: 3.162

8.  Amino acid variant in the kinase binding domain of dual-specific A kinase-anchoring protein 2: a disease susceptibility polymorphism.

Authors:  Stefan Kammerer; Lora L Burns-Hamuro; Yuliang Ma; Sara C Hamon; Jaume M Canaves; Michael M Shi; Matthew R Nelson; Charles F Sing; Charles R Cantor; Susan S Taylor; Andreas Braun
Journal:  Proc Natl Acad Sci U S A       Date:  2003-03-19       Impact factor: 11.205

9.  Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain.

Authors:  F Les Erickson; Amoreena C Corsa; Andrea C Dose; Beth Burnside
Journal:  Mol Biol Cell       Date:  2003-07-25       Impact factor: 4.138

10.  Stereochemical preferences modulate affinity and selectivity among five PDZ domains that bind CFTR: comparative structural and sequence analyses.

Authors:  Jeanine F Amacher; Patrick R Cushing; Lionel Brooks; Prisca Boisguerin; Dean R Madden
Journal:  Structure       Date:  2013-11-07       Impact factor: 5.006

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.