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A common mechanism for posttranslational activation of plasma membrane receptors?
Author(s) -
Olson Tracy S.,
Lane M. Daniel
Publication year - 1989
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.3.5.2537774
Subject(s) - endoplasmic reticulum , receptor , microbiology and biotechnology , chemistry , ligand (biochemistry) , protein subunit , biophysics , biochemistry , biology , gene
The process for posttranslational acquisition of ligand binding function is remarkably similar for three receptors with dissimilar structures, namely, the insulin, epidermal growth factor, and acetylcholine receptors. These receptors lack the ability to bind ligand immediately after translation, but slowly ( t 1/2 = 30‐45 min) acquire this capacity while in the endoplasmic reticulum. This activation step occurs with similar kinetics for all three receptors and, in each case, requires N‐linked glycosylation. Several lines of evidence suggest a common mechanism for the acquisition of ligand binding function that involves the rearrangement of metastable disulfide bonds formed during or immediately after translation. This process precedes subunit assembly of both insulin and acetylcholine receptors, which also occurs in the endoplasmic reticulum. The posttranslational processing steps leading to the acquisition of ligand binding function may be an example of a more general process affecting cell surface proteins.— O lson , T. S.; L ane , M. D. A common mechanism for posttranslational activation of plasma membrane receptors? FASEB J. 3: 1618‐1624; 1989.