AI Insight
Two recent studies published in PLOS Biology reveal structural details of SLC37A4, the human glucose-6-phosphate transporter that moves glucose-6-phosphate into the endoplasmic reticulum. These structural snapshots, combined with other research reports, provide insight into how the protein cycles between different conformations to exchange glucose-6-phosphate for phosphate across the membrane, and how this process can be inhibited. Understanding these structures helps explain the molecular mechanism underlying glucose homeostasis regulation in human cells.
Why it matters
SLC37A4 plays a critical role in maintaining blood glucose levels, and its dysfunction is associated with glycogen storage disease type 1b. Structural knowledge of this transporter and its inhibition mechanism could inform the development of therapeutic approaches for metabolic disorders related to glucose regulation.
Understand the Science
by Lin Kevin Qi, Cheng Shen, Motoyuki Hattori
SLC37A4 mediates glucose-6-phosphate transport for glucose homeostasis. Two recent studies in PLOS Biology report its structures and, together with other reports, illuminate the glucose-6-phosphate/phosphate exchange cycle and its inhibition mechanism.
The human glucose-6-phosphate transporter (SLC37A4) mediates the translocation of G6P into the ER. Two recent studies in PLOS Biology report its structures and, together with other reports, illuminate the glucose-6-phosphate/phosphate exchange cycle and its inhibition mechanism.
Source: Structural snapshots of the glucose-6-phosphate/phosphate exchange cycle