Oligomerization of pro‐opiomelanocortin is independent of pH, calcium and the sorting signal for the regulated secretory pathway

FEBS Letters

Chen, Anthony¹  Cawley, Niamh X¹  Normant, Emmanuel¹  Loh, Y.Peng¹ 

[1] Section on Cellular Neurobiology, Laboratory of Developmental Neurobiology, Bldg. 49/Rm 5A38, National Institute for Child and Human Development, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Pro-opiomelanocortin;    Oligomerization;    Aggregation;    Prohormone sorting;   

DOI  :  10.1016/S0014-5793(00)01961-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown