The Pseudo signal peptide of the corticotropin-releasing factor receptor type 2A prevents receptor oligomerization.

ABSTRACT: N-terminal signal peptides mediate the interaction of native proteins with the translocon complex of the endoplasmic reticulum membrane and are cleaved off during early protein biogenesis. The corticotropin-releasing factor receptor type 2a (CRF(2(a))R) possesses an N-terminal pseudo signal peptide, which represents a so far unique domain within the large protein family of G protein-coupled receptors (GPCRs). In contrast to a conventional signal peptide, the pseudo signal peptide remains uncleaved and consequently forms a hydrophobic extension at the N terminus of the receptor. The functional consequence of the presence of the pseudo signal peptide is not understood. Here, we have analyzed the significance of this domain for receptor dimerization/oligomerization in detail. To this end, we

SUBMITTER: Teichmann A 

PROVIDER: S-EPMC3411068 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature