Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2006 Aug;1761(8):947-56. Epub 2006 Apr 27.

The prevalence and significance of PDZ domain-phosphoinositide interactions.

Author information

1
Department of Human Genetics, University of Leuven and Flanders Interuniversity Institute for Biotechnology, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium. pascale.zimmermann@med.kuleuven.be

Abstract

PDZ domains predominate in multi-cellular organisms. They are ubiquitous protein-interaction modules recognizing short peptide sequences generally situated at the C-terminal end of plasma membrane proteins. They contribute to the formation and spatial confinement of protein complexes and thereby play an essential role in the control of cell signaling. Recent studies indicate that PDZ domains can also interact with phosphoinositides (PIPs), signaling lipids with key-roles in receptor signal transduction, membrane trafficking, cytoskeleton remodeling and nuclear processes. In particular the PDZ domains of syntenin-1 and syntenin-2 bind to phosphatidylinositol 4, 5-bisphosphate (PIP2) with high-affinity. Syntenin-1/PIP2 interaction is important for receptor cargo recycling and syntenin-2 plays a role in the organization of nuclear PIP2. In addition, other lower-affinity PDZ domain/PIPs interactions are documented. Here, we summarize and discuss the present knowledge about the occurrence, the biochemistry and the biology of PDZ domain-lipid interactions.

PMID:
16884951
DOI:
10.1016/j.bbalip.2006.04.003
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center