Yong Wei et al. present the crystal structure of the human lysosomal protein EPDR1 and reveal a role in lipid-binding. They show that the larger family of ependymin-related proteins adopt a β-sheet fold previously seen only in bacterial proteins, and that this fold is found throughout the archaea and eukaryotes.

The distribution of lipids largely depends on their non-vesicular transport by lipid transfer proteins (LTPs). Recent progress in understanding the mechanisms of LTPs, including the appreciation of their widespread activity at membrane contact sites, has provided novel insights into the regulation of lipid trafficking and how it impacts pathophysiology.

Cation/proton antiporters (CPAs) play a major role in maintaining living cells’ homeostasis and are divided in two main groups: CPA1 and CPA2. Here authors use a comprehensive evolutionary analysis of 6537 representative CPAs and reveal a sequence motif that determines central phenotypic characteristics.

Endoplasmic reticulum (ER) functioning requires a constant supply of ATP, but the exchanger required for ATP uptake into the ER is unknown. Here, the authors report that SLC35B1, here named AXER, or ATP/ADP exchanger into the ER, can transport ATP into the ER.