Article
Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins.
The Journal of biological chemistry - 6 Aug 1999
Espenshade P J, Cheng D, Goldstein J L, Brown M S
Abstract excerpt
Site-1 protease (S1P) is a subtilisin-related protease that cleaves sterol regulatory element-binding proteins (SREBPs) in the endoplasmic reticulum lumen, thereby initiating a process by which the transcriptionally active NH(2)-terminal fragments of SREBPs are released from membranes. In the current experiments, we transfected cDNAs encoding epitope-tagged hamster S1P into HEK-293 cells or mutant hamster cells...
Topics
- Amino Acid Sequence
- Animals
- Cholesterol
- Cricetinae
- DNA-Binding Proteins
- Enzyme Activation
- Hydroxycholesterols
- Intracellular Signaling Peptides and Proteins
- Membrane Proteins
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Precipitin Tests