Signaling and subcellular targeting by membrane-binding domains

Protein kinase C homology-1 and -2, FYVE, and pleckstrin homology domains a re ubiquitous in eukaryotic signal transduction and membrane-trafficking pr oteins. These domains regulate subcellular localization and protein functio n by binding to lipid ligands embedded in cell membranes. Structural and bi ochemical analysis of these domains has shown that their molecular mechanis ms of membrane binding depend on a combination of specific and nonspecific interactions with membrane lipids. In vivo studies of green fluorescent pro tein fusions have highlighted the key roles of these domains in regulating protein localization to plasma and internal membranes in cells.