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N端天冬氨酸在神经肽Y Y2受体内化中的重要性。

Importance of a N-terminal aspartate in the internalization of the neuropeptide Y Y2 receptor.

作者信息

Parker Steven L, Parker Michael S, Wong Ying Y, Sah Renu, Balasubramaniam Ambikaipakan, Sallee Floyd

机构信息

Department of Pharmacology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.

出版信息

Eur J Pharmacol. 2008 Oct 10;594(1-3):26-31. doi: 10.1016/j.ejphar.2008.07.038. Epub 2008 Jul 30.

DOI:10.1016/j.ejphar.2008.07.038
PMID:18700141
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2579264/
Abstract

With human neuropeptide Y Y2 receptor expressed in the Chinese hamster ovary (CHO) cells, the Asp35Ala mutation, and especially the change of Pro34Asp35 to Ala34Ala35, decrease the compartmentalization and strongly accelerate internalization of the receptor. These changes are not associated with alterations in agonist affinity, G-protein interaction, dimerization, or level of expression of the mutated receptors relative to the wildtype receptor. The proline-flanked aspartate in the N-terminal extracellular segment of the neuropeptide Y Y2 receptor thus apparently has a large role in anchoring and compartmentalization of the receptor. However, the Pro34Ala mutation does not significantly affect the embedding and cycling of the receptor.

摘要

在中国仓鼠卵巢（CHO）细胞中表达的人神经肽Y Y2受体，Asp35Ala突变，尤其是Pro34Asp35变为Ala34Ala35，会减少受体的区室化并强烈加速其内化。这些变化与激动剂亲和力、G蛋白相互作用、二聚化或突变受体相对于野生型受体的表达水平改变无关。因此，神经肽Y Y2受体N端细胞外段中脯氨酸侧翼的天冬氨酸显然在受体的锚定和区室化中起很大作用。然而，Pro34Ala突变对受体的嵌入和循环没有显著影响。

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