An unexpected battle with peripartum cardiomyopathy: a case report.

Peripartum cardiomyopathy (PPCM) is a rare cardiomyopathy marked by systolic dysfunction that presents in late pregnancy or the early postpartum period with an ejection fraction (EF) of less than 45%. Diagnosing PPCM often presents a diagnostic dilemma due to its nonspecific clinical presentation, which usually resembles physiological changes of pregnancy or peripartum pulmonary embolism. Echocardiography is frequently used as a diagnostic modality of choice with management following the GDMT guidelines and delivery.

Conserved Pib2 regions have distinct roles in TORC1 regulation at the vacuole.

TORC1 is a critical controller of cell growth in eukaryotes. In yeast (Saccharomyces cerevisiae), the presence of nutrients is signaled to TORC1 by several upstream regulatory sensors that together coordinate TORC1 activity. TORC1 localizes to both vacuolar and endosomal membranes, where differential signaling occurs.

The cryo-EM structure of the SNX-BAR Mvp1 tetramer.

Sorting nexins (SNX) are a family of PX domain-containing proteins with pivotal roles in trafficking and signaling. SNX-BARs, which also have a curvature-generating Bin/Amphiphysin/Rvs (BAR) domain, have membrane-remodeling functions, particularly at the endosome. The minimal PX-BAR module is a dimer mediated by BAR-BAR interactions.

Feedback regulation of TORC1 by its downstream effectors Npr1 and Par32.

TORC1 (target of rapamycin complex) integrates complex nutrient signals to generate and fine-tune a growth and metabolic response. Npr1 (nitrogen permease reactivator) is a downstream effector kinase of TORC1 that regulates the stability, activity, and trafficking of various nutrient permeases including the ammonium permeases Mep1, Mep2, and Mep3 and the general amino acid permease Gap1. Npr1 exerts its regulatory effects on Mep1 and Mep3 via Par32 (phosphorylated after rapamycin).

Ivy1 is a negative regulator of Gtr-dependent TORC1 activation.

The highly conserved TORC1 complex controls cell growth in response to nutrients, especially amino acids. The EGO complex activates TORC1 in response to glutamine and leucine. Here, we demonstrate that the I-BAR domain-containing protein Ivy1 colocalizes with Gtr1 and Gtr2, a heterodimer of small GTPases that are part of the EGO complex.

Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture.

Dynamin-related proteins (DRPs) are large multidomain GTPases required for diverse membrane-remodeling events. DRPs self-assemble into helical structures, but how these structures are tailored to their cellular targets remains unclear. We demonstrate that the fungal DRP Vps1 primarily localizes to and functions at the endosomal compartment.