▪ Abstract Research in the past decade has revealed that many cytosolic proteins are
recruited to different cellular membranes to form protein-protein and lipid-protein interactions …

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane
glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including …

The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer
predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and …

Abstract The phospholipase A 2 (PLA 2) superfamily consists of many different groups of
enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different …

The Group IV phospholipase A2 family is comprised of six intracellular enzymes commonly
called cytosolic phospholipase A2 (cPLA2) α, cPLA2β, cPLA2γ, cPLA2δ, cPLA2ε and …

PTEN is a tumor suppressor that reverses the action of phosphoinositide 3-kinase by
catalyzing the removal of the 3′ phosphate of phosphoinositides. Despite the critical role of …

The C2 domain acts as a membrane‐targeting module in a diverse group of proteins
including classical protein kinase Cs (PKCs), where it plays an essential role in activation …

C2 domains are a ubiquitous structural module and many of them function in Ca2+-
dependent membrane binding and thereby serve as Ca2+ effectors for divergent Ca2+ …

▪ Abstract Protein kinase C homology-1 and-2, FYVE, and pleckstrin homology domains are
ubiquitous in eukaryotic signal transduction and membrane-trafficking proteins. These …

During the last decade there has been significant progress in the development of analytical
techniques for the screening of ligand binding to membranes and membrane receptors. This …