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Oligomerization of pro‐opiomelanocortin is independent of pH, calcium and the sorting signal for the regulated secretory pathway
Author(s) -
Cawley Niamh X,
Normant Emmanuel,
Chen Anthony,
Loh Y.Peng
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01961-x
Subject(s) - chemistry , sorting , microbiology and biotechnology , calcium , receptor , biochemistry , carboxypeptidase , secretion , biophysics , biology , enzyme , organic chemistry , computer science , programming language
Studies indicate that pro‐opiomelanocortin (POMC) is sorted to the regulated secretory pathway by binding to a sorting receptor identified as membrane‐bound carboxypeptidase E (CPE) [Cool et al. (1997) Cell 88, 73–83]. The efficiency of this sorting mechanism could be enhanced if POMC molecules were to self‐associate to form oligomers, prior or subsequent to binding to CPE. Using cross‐linking and gel filtration techniques, we demonstrated that POMC forms oligomers at both neutral and acidic pHs and calcium was not necessary. ΔN‐POMC, which lacks the N‐terminal sorting signal for the regulated secretory pathway, also formed similar oligomers, indicating that the sorting and oligomerization domains are different.