ArticleMolecular biology of the cell2004
The palmitoyltransferase of the cation-dependent mannose 6-phosphate receptor cycles between the plasma membrane and endosomes.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023Review
- Review
- Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family.Plant physiology · 2012Article
- The palmitoyl transferase DHHC2 targets a dynamic membrane cycling pathway: regulation by a C-terminal domain.Molecular biology of the cell · 2011Article
- The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum.The Journal of biological chemistry · 2011Article
- On the role of acylation of transmembrane proteins.Biophysical journal · 2010Article
- Palmitoylation controls recycling in lysosomal sorting and trafficking.Traffic (Copenhagen, Denmark) · 2008Article
- Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Sequence requirements for localization of human cytomegalovirus tegument protein pp28 to the virus assembly compartment and for assembly of infectious virus.Journal of virology · 2006Article
- The human Kv1.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cation-dependent mannose 6-phosphate receptor (CD-MPR) mediates the transport of lysosomal enzymes from the trans-Golgi network to endosomes. Evasion of lysosomal degradation of the CD-MPR requires reversible palmitoylation of a cysteine residue in its cytoplasmic tail. Because palmitoylation is reversible and essential for correct trafficking, it presents a potential regulatory mechanism for the sorting signals within the cytoplasmic domain of the CD-MPR. Characterization of the palmitoylation performing an in vitro palmitoylation assay by using purified full-length CD-MPR revealed that palmitoylation of the CD-MPR occurs enzymatically by a membrane-bound palmitoyltransferase. In addition, analysis of the localization revealed that the palmitoyltransferase cycles between endosomes and the plasma membrane. This was identified by testing fractions from HeLa cell homogenate separated on a density gradient in the in vitro palmitoylation assay and further confirmed by in vivo labeling experiments by using different treatments to block specific protein trafficking steps within the cell. We identified a novel palmitoyltransferase activity in the endocytic pathway responsible for palmitoylation of the CD-MPR. The localization of the palmitoyltransferase not only fulfills the requirement of our hypothesis to be a regulator of the intracellular trafficking of the CD-MPR but also may affect the sorting/activity of other receptors cycling through endosomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.