Structure and regulation of phospholipase Cβ and ε at the membrane.

Phospholipase C (PLC) β and ε enzymes hydrolyze phosphatidylinositol (PI) lipids in response to direct interactions with heterotrimeric G protein subunits and small GTPases, which are activated downstream of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). PI hydrolysis generates second messengers that increase the intracellular Ca concentration and activate protein kinase C (PKC), thereby regulating numerous physiological processes. PLCβ and PLCε share a highly conserved core required for lipase activity, but use different strategies and structural elements to autoinhibit basal activity, bind membranes, and engage G protein activators.

Structure of phospholipase Cε reveals an integrated RA1 domain and previously unidentified regulatory elements.

Phospholipase Cε (PLCε) generates lipid-derived second messengers at the plasma and perinuclear membranes in the cardiovascular system. It is activated in response to a wide variety of signals, such as those conveyed by Rap1A and Ras, through a mechanism that involves its C-terminal Ras association (RA) domains (RA1 and RA2). However, the complexity and size of PLCε has hindered its structural and functional analysis.

Voiding Cystourethrogram in Children With Unilateral Multicystic Dysplastic Kidney: Is It Still necessary?

Objective: To evaluate the value of the voiding cystourethrogram (VCUG) in children with multicystic dysplastic kidney (MCDK) who have a normal versus abnormal contralateral kidney and bladder ultrasound (US), and assess the risk of having vesicoureteral reflux (VUR) or urinary tract infection (UTI) based on the US results.

Methods: A retrospective chart review including children with unilateral MCDK with postnatal US and VCUG available at our institution between January 2008 and September 2017 was performed. Analysis was done to find association between abnormal contralateral US and contralateral VUR and UTI.