TY - JOUR
T1 - Depalmitoylation and cell physiology
T2 - APT1 as a mediator of metabolic signals
AU - Speck, Sarah L.
AU - Wei, Xiaochao
AU - Semenkovich, Clay F.
N1 - Publisher Copyright:
© 2024 the American Physiological Society.
PY - 2024/4
Y1 - 2024/4
N2 - More than half of the global population is obese or overweight, especially in Western countries, and this excess adiposity disrupts normal physiology to cause chronic diseases. Diabetes, an adiposity-associated epidemic disease, affects >500 million people, and cases are projected to exceed 1 billion before 2050. Lipid excess can impact physiology through the posttranslational modification of proteins, including the reversible process of S-palmitoylation. Dynamic palmitoylation cycling requires the S-acylation of proteins by acyltransferases and the depalmitoylation of these proteins mediated in part by acyl-protein thioesterases (APTs) such as APT1. Emerging evidence points to tissue-specific roles for the depalmitoylase APT1 in maintaining homeostasis in the vasculature, pancreatic islets, and liver. These recent findings raise the possibility that APT1 substrates can be therapeutically targeted to treat the complications of metabolic diseases.
AB - More than half of the global population is obese or overweight, especially in Western countries, and this excess adiposity disrupts normal physiology to cause chronic diseases. Diabetes, an adiposity-associated epidemic disease, affects >500 million people, and cases are projected to exceed 1 billion before 2050. Lipid excess can impact physiology through the posttranslational modification of proteins, including the reversible process of S-palmitoylation. Dynamic palmitoylation cycling requires the S-acylation of proteins by acyltransferases and the depalmitoylation of these proteins mediated in part by acyl-protein thioesterases (APTs) such as APT1. Emerging evidence points to tissue-specific roles for the depalmitoylase APT1 in maintaining homeostasis in the vasculature, pancreatic islets, and liver. These recent findings raise the possibility that APT1 substrates can be therapeutically targeted to treat the complications of metabolic diseases.
KW - acyl-protein thioesterase
KW - diabetes
KW - insulin
KW - obesity
KW - S-acylation
UR - http://www.scopus.com/inward/record.url?scp=85187692998&partnerID=8YFLogxK
U2 - 10.1152/ajpcell.00542.2023
DO - 10.1152/ajpcell.00542.2023
M3 - Review article
C2 - 38344800
AN - SCOPUS:85187692998
SN - 0363-6143
VL - 326
SP - C1034-C1041
JO - American Journal of Physiology - Cell Physiology
JF - American Journal of Physiology - Cell Physiology
IS - 4
ER -