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Updated: May 21, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
Published on: July 27, 2017
Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms
Klaus Scheffzek1, Stefan Welti
1Division Biological Chemistry, Biocenter, Innsbruck Medical University, Innrain 80/82, A-6020 Innsbruck, Austria. Klaus.Scheffzek@i-med.ac.at
Abstract:
The initial reports on pleckstrin homology (PH) domains almost 20 years ago described them as sequence feature of proteins involved in signal transduction processes. Investigated at first along the phospholipid binding properties of a small subset of PH representatives, the PH fold turned out to appear as mediator of phosphotyrosine and polyproline peptide binding to other signaling proteins. While phospholipid binding now seems rather the exception among PH-like domains, protein-protein interactions established as more and more important feature of these modules. In this review we focus on the PH superfold as a versatile protein-protein interaction platform and its three-dimensional integration in an increasing number of available multidomain structures.
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