Article
Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid.
The Journal of biological chemistry - 25 Sept 1990
Alvarez E, Gironès N, Davis R J
Abstract excerpt
The human transferrin receptor is post-translationally modified by the covalent attachment of palmitic acid to Cys62 and Cys67 via a thio-ester bond. To investigate the role of the acylation of the transferrin receptor, Cys62 and Cys67 were substituted with serine and alanine residues. The proper...
Topics
- Acylation
- Amino Acid Sequence
- Animals
- Base Sequence
- Cell Line
- Chromosome Deletion
- Cystine
- Endocytosis
- Humans
- Kinetics
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Palmitic Acid
- Palmitic Acids
- Protein Processing, Post-Translational
- Receptors, Transferrin
- Transfection