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Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone

We have identified 88 interactor candidates for human growth hormone (GH) by the yeast two-hybrid assay. Among those, we focused our efforts on carboxypeptidase E (CPE), which has been thought to play a key role in sorting prohormones, such as pro-opiomelanocortin (POMC), to regulated secretory vesi...

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Bibliographic Details
Published in:Molecules and cells 2016, 39(10), , pp.756-761
Main Authors: Mizutani, Akiko, Inoko, Hidetoshi, Tanaka, Masafumi
Format: Article
Language:English
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Summary:We have identified 88 interactor candidates for human growth hormone (GH) by the yeast two-hybrid assay. Among those, we focused our efforts on carboxypeptidase E (CPE), which has been thought to play a key role in sorting prohormones, such as pro-opiomelanocortin (POMC), to regulated secretory vesicles. We found that CPE co-localizes with and interacts with GH in AtT20 pituitary cells. Downregulation of CPE led to decreased levels of GH secretion, consistent with involvement of CPE in GH sorting/secretion. Our binding assay with bacterially expressed proteins suggested that GH directly interacts with CPE but in a manner different from POMC.
ISSN:1016-8478
0219-1032
DOI:10.1016/molcells.2016.0183