Abstract：
:Accumulating evidence suggests that the human follitropin receptor is unusually sensitive to mutation. Previous results (Mol. Cell. Endo. 166 (2000) 101) determined that scanning mutations in a.a. 12-14 and 22-30 neither bound follitropin nor were present on the cell surface, suggesting that these regions are involved in either hormone binding or trafficking. To distinguish between these hypotheses, single alanine substitutions in a.a. 12-14 and 22-30 were generated, all of which appeared to bind 125I-follitropin with an affinity constant similar to wild type (wt) follitropin receptor. However, the level of receptor on the cell surface varied widely, in some cases 100-fold lower than wt. Expression on the cell surface corresponded to expression of the mature 80 kD follitropin receptor. An accumulation of the ER-resident 62 kD band of follitropin receptor was observed in mutants that had low surface expression of receptor, suggesting that misfolded protein was trapped in the ER by a quality control mechanism.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Nechamen CA,Dias JAdoi
10.1016/s0303-7207(02)00424-0keywords:
subject
Has Abstractpub_date
2003-03-28 00:00:00pages
123-31issue
1-2eissn
0303-7207issn
1872-8057pii
S0303720702004240journal_volume
201pub_type
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