PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions

1998/06/01 by Mario J. Rebecchi, Suzanne Scarlata · 2 citations
Biochemistry, Genetics and Molecular Biology · Materials Science · #Glycosylation and Glycoproteins Research #Ubiquitin and proteasome pathways #Enzyme Structure and Function

paper · doi:10.1146/annurev.biophys.27.1.503

openalex publication_date 1998/06/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

Pleckstrin homology (PH) motifs are approximately 100 amino-acid residues long and have been identified in nearly 100 different eukaryotic proteins, many of which participate in cell signaling and cytoskeletal regulation. Despite minimal sequence homology, the three-dimensional structures are remarkably conserved. This review gives an overview of the PH domain architecture and examines the best-studied examples in an attempt to understand their function.

Citations

• Membrane Binding of Phospholipases C-β1 and C-β2 Is Independent of Phosphatidylinositol 4,5-Bisphosphate and the α and βγ Subunits of G Proteins

Cited by

• The membrane and lipids as integral participants in signal transduction: lipid signal transduction for the non-lipid biochemist
• Suzanne Scarlata [wikipedia]