Article open access publication

Membrane Binding and Modulation of the PDZ Domain of PICK1

Membranes, MDPI, ISSN 2077-0375

Volume 5, 4, 2015

DOI:10.3390/membranes5040597, Dimensions: pub.1008904248, PMC: PMC4704001, PMID: 26501328,

Affiliations

Organisations

  1. (1) University of Copenhagen, grid.5254.6, KU

Countries

Denmark

Continents

Europe

Description

Scaffolding proteins serve to assemble protein complexes in dynamic processes by means of specific protein-protein and protein-lipid binding domains. Many of these domains bind either proteins or lipids exclusively; however, it has become increasingly evident that certain domains are capable of binding both. Especially, many PDZ domains, which are highly abundant protein-protein binding domains, bind lipids and membranes. Here we provide an overview of recent large-scale studies trying to generalize and rationalize the binding patterns as well as specificity of PDZ domains towards membrane lipids. Moreover, we review how these PDZ-membrane interactions are regulated in the case of the synaptic scaffolding protein PICK1 and how this might affect cellular localization and function.

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University of Copenhagen

Dimensions Citation Indicators

Times Cited: 8

Field Citation Ratio (FCR): 1.57

Relative Citation ratio (RCR): 0.25

Open Access Info

Pure Gold