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Phosphoinositides and PDZ Domain Scaffolds

  • Anna Maria Wawrzyniak
  • Rudra Kashyap
  • Pascale Zimmermann
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 991)

Abstract

The discovery that PSD-95/Discs large/ZO-1 (PDZ) domains can function as lipid-binding modules, in particular interacting with phosphoinositides (PIs), was made more than 10 years ago (Mol Cell 9(6): 1215–1225, 2002). Confirmatory studies and a series of functional follow-ups established PDZ domains as dual specificity modules displaying both peptide and lipid binding, and prompted a rethinking of the mode of action of PDZ domains in the control of cell signaling. In this chapter, after introducing PDZ domains, PIs and methods for studying protein-lipid interactions, we focus on (i) the prevalence and the specificity of PDZ-PIs interactions, (ii) the molecular determinants of PDZ-PIs interactions, (iii) the integration of lipid and peptide binding by PDZ domains, (iv) the common features of PIs interacting PDZ domains and (v) the regulation and functional significance of PDZ-PIs interactions.

Keywords

Scaffold Cell signaling Protein-lipid interactions Dual specificity modules Nucleus 

Notes

Acknowledgments

The laboratories of P.Z. are supported by the Fund for Scientific Research-Flanders (FWO), the Concerted Actions Program of the Katholieke Universiteit Leuven, the Belgian Federation Against Cancer (Stichting Tegen Kanker), the Interuniversity Attraction poles of the Prime Ministers Services (IUAP), and the EMBO young investigator program (to P.Z.). A.M.W. is supported by a Ph.D. fellowship from FWO.

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Anna Maria Wawrzyniak
    • 1
  • Rudra Kashyap
    • 1
    • 2
    • 3
    • 4
    • 5
  • Pascale Zimmermann
    • 1
    • 2
    • 3
    • 4
    • 5
  1. 1.Department of Human GeneticsKULeuvenLeuvenBelgium
  2. 2.Inserm, U1068, CRCMMarseilleFrance
  3. 3.Institut Paoli-CalmettesMarseilleFrance
  4. 4.Aix-Marseille UniversityF-13284France
  5. 5.CNRS, UMR7258, CRCMMarseilleFrance

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