Transformation of the signal peptide/membrane anchor domain of a type II transmembrane protein into a cleavable signal peptide.
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 268, Issue: 4, Page: 2699-2704
1993
- 16Citations
- 7Captures
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Metrics Details
- Citations16
- Citation Indexes16
- CrossRef16
- Captures7
- Readers7
Abstract Description
Rabbit neutral endopeptidase-24.11 is a type II transmembrane protein with a 27-amino acid residue positively charged NH2-terminal cytoplasmic domain, a 23-amino acid residue hydrophobic signal peptide/membrane anchor domain, and a large catalytic COOH-terminal domain exposed on the exoplasmic side of the membrane. In order to study the mechanism of membrane anchoring of neutral endopeptidase-24.11, we created mutants in which the cytoplasmic tail was deleted. Expression of these mutants in COS-1 cells resulted in the secretion of approximately 10-20% of the protein into the culture medium, due possibly to the cleavage of part or all of the signal peptide/membrane anchor domain by the rough endoplasmic reticulum signal peptidase. In a second set of mutants, a hydrophilic sequence (GSQNS) was inserted midway in the signal peptide/membrane anchor domain of neutral endopeptidase-24.11. When this hydrophilic sequence was introduced into the full-length neutral endopeptidase-24.11, approximately 20% of the enzyme activity was recovered in the culture medium. This proportion increased to 93% when the cytosolic tail was deleted. Sequencing of the [3H]tyrosine- or [3H]isoleucine-labeled secreted protein indicated that proteolysis, possibly by signal peptidase, occurred on the COOH-terminal side of the signal peptide/membrane anchor domain. We conclude that the efficient cleavage of the signal peptide/membrane anchor domain and secretion of the protein require both the deletion of the cytosolic domain and the presence of a hydrophilic sequence.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818538308; http://dx.doi.org/10.1016/s0021-9258(18)53830-8; https://linkinghub.elsevier.com/retrieve/pii/S0021925818538308; https://api.elsevier.com/content/article/PII:S0021925818538308?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0021925818538308?httpAccept=text/plain; https://dul.usage.elsevier.com/doi/; http://dx.doi.org/10.1016/s0021-9258%2818%2953830-8; https://dx.doi.org/10.1016/s0021-9258%2818%2953830-8
Elsevier BV
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