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Am J Physiol Heart Circ Physiol (March 7, 2002). doi:10.1152/ajpheart.00008.2002
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Articles in PresS, published online ahead of print March 7, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00008.2002
Submitted on January 8, 2002
Accepted on February 25, 2002

Role of Glycosylation in the Cell Surface Expression and Stability of HERG Potassium Channels

Qiuming Gong, Corey L Anderson, Craig T January, and Zhengfeng Zhou*

* To whom correspondence should be addressed. E-mail: zhouzh{at}ohsu.edu.

The human ether-a-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel, IKr, in the heart. We have previously shown that HERG channel protein is modified by N-linked glycosylation. HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629). In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels. Our results show that N598 is the only site for N-linked glycosylation and glycosylation is not required for the cell surface expression of functional HERG channels. In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention. Pulse-chase experiments show that the turnover rate of unglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.




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