STRUCTURAL VIEWS OF PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C - SIGNALING THE WAY AHEAD

Recent structural studies of mammalian phosphoinositide-specific phosp holipase C (PI-PLC) have begun to shed light on the mechanism whereby this family of effector enzymes is able to hydrolyze phospholipid subs trates to yield second messengers. PI-PLC isozymes employ a variety of modules (PH domain, EF-hand domain, SH2 domain, SH3 domain and C2 dom ain) that are common in proteins involved in signal transduction to re versibly interact with membranes and protein components of the signall ing pathways.