期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 4, 页码 2841-2851出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M005700200
关键词
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资金
- NIGMS NIH HHS [GM 56337] Funding Source: Medline
Two neuregulin-1 isoforms highly expressed in the nervous system are the type III neuregulin III-beta 1a and the type I neuregulin I-beta 1a The sequence of these two isoforms differs only in the region that is N-terminal of the bioactive epidermal growth factor-like domain. While the biosynthetic processing of the I-beta 1a isoform has been well characterized, the processing of III-beta 1a has not been reported. In this study, we compared III-beta 1a and I-beta 1a processing. Both III-beta 1a and I-beta 1a were synthesized as transmembrane proproteins that were proteolytically cleaved to produce an N-terminal fragment containing the bioactive epidermal growth factor-like domain. For I-beta 1a, this product was released into the medium. However, for III-beta 1a, this product was a transmembrane protein. In cultures of cells expressing III-beta 1a, the amount of neuregulin at the cell surface was much greater, and the amount in the medium was much less than in cultures expressing I-beta 1a Phorbol eater treatment and truncation of the cytoplasmic tail had markedly different effects on III-beta 1a and I-beta 1a processing. These results demonstrate an important role for the N-terminal region in determining neuregulin biosynthetic processing and show that a major product of III-beta 1a processing is a tethered ligand that may act as a cell surface signaling molecule.
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