糖基化
N-连接糖基化
受体
生物化学
化学
定点突变
突变
黑色素浓缩激素
细胞生物学
生物
糖蛋白
聚糖
突变
基因
突变体
神经肽
作者
Yumiko Saito,Mitsue Tetsuka,Yue Li,Yuuki Kawamura,Kei Maruyama
出处
期刊:FEBS Letters
[Wiley]
日期:2002-12-03
卷期号:533 (1): 29-34
被引量:36
标识
DOI:10.1016/s0014-5793(02)03744-4
摘要
Melanin‐concentrating hormone (MCH) is known to act through two G‐protein‐coupled receptors MCHR1 and MCHR2. MCHR1 has three potential sites (Asn 13 , Asn 16 and Asn 23 ) for N ‐linked glycosylation in its extracellular amino‐terminus which may modulate its reactivity. Site‐directed mutagenesis of the rat MCHR1 cDNA at single or multiple combinations of the three potential glycosylation sites was used to examine the role of the putative carbohydrate chains on receptor activity. It was found that all three potential N ‐linked glycosylation sites in MCHR1 were glycosylated, and that N ‐linked glycosylation of Asn 23 was necessary for full activity. Furthermore, disruption of all three glycosylation sites impaired proper expression at the cell surface and receptor activity. These data outline the importance of the N ‐linked glycosylation of the MCHR1.
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