TY - JOUR
T1 - Palmitoylation controls recycling in lysosomal sorting and trafficking
AU - McCormick, Peter J.
AU - Dumaresq-Doiron, Karine
AU - Pluviose, Anne-Sophie
AU - Pichette, Vincent
AU - Tosato, Giovanna
AU - Lefrancois, Stephane
PY - 2008/1/1
Y1 - 2008/1/1
N2 - For the efficient trafficking of lysosomal proteins, the cationic-dependent and -independent mannose 6-phosphate receptors and sortilin must bind cargo in the Golgi apparatus, be packaged into clathrin-coated trafficking vesicles and traffic to the endosomes. Once in the endosomes, the receptors release their cargo into the endosomal lumen and recycle back to the Golgi for another round of trafficking, a process that requires retromer. In this study, we demonstrate that palmitoylation is required for the efficient retrograde trafficking of sortilin, and the cationic-independent mannose 6-phosphate as palmitoylation-deficient receptors remain trapped in the endosomes. Importantly, we also show that palmitoylation is required for receptor interaction with retromer as nonpalmitoylated receptor did not interact with retromer. In addition, we have identified DHHC-15 as the palmitoyltransferase responsible for this modification. In summary, we have shown the functional significance of palmitoylation in lysosomal receptor sorting and trafficking.
AB - For the efficient trafficking of lysosomal proteins, the cationic-dependent and -independent mannose 6-phosphate receptors and sortilin must bind cargo in the Golgi apparatus, be packaged into clathrin-coated trafficking vesicles and traffic to the endosomes. Once in the endosomes, the receptors release their cargo into the endosomal lumen and recycle back to the Golgi for another round of trafficking, a process that requires retromer. In this study, we demonstrate that palmitoylation is required for the efficient retrograde trafficking of sortilin, and the cationic-independent mannose 6-phosphate as palmitoylation-deficient receptors remain trapped in the endosomes. Importantly, we also show that palmitoylation is required for receptor interaction with retromer as nonpalmitoylated receptor did not interact with retromer. In addition, we have identified DHHC-15 as the palmitoyltransferase responsible for this modification. In summary, we have shown the functional significance of palmitoylation in lysosomal receptor sorting and trafficking.
UR - http://www.scopus.com/inward/record.url?scp=53849122301&partnerID=8YFLogxK
U2 - 10.1111/j.1600-0854.2008.00814.x
DO - 10.1111/j.1600-0854.2008.00814.x
M3 - Article
AN - SCOPUS:53849122301
SN - 1398-9219
VL - 9
SP - 1984
EP - 1997
JO - Traffic
JF - Traffic
IS - 11
ER -