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The N terminus and transmembrane segment S1 of Kv1.5 can coassemble with the rest of the channel independently of the S1–S2 linkage

  • Published:2018-10 Issue:40 Volume:293 Page:15347-15358
  • ISSN:0021-9258
  • Container-title:Journal of Biological Chemistry
  • language:en
  • Short-container-title:Journal of Biological Chemistry

Author:

Lamothe Shawn M.,Hogan-Cann Aja E.,Li Wentao,Guo Jun,Yang Tonghua,Tschirhart Jared N.,Zhang Shetuan

Funder

Government of Canada | Natural Sciences and Engineering Research Council of Canada (NSERC)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Ubiquitination is involved in PKC-mediated degradation of cell surface Kv1.5 channels;Journal of Biological Chemistry;2024-07

2. Novel Loss-of-Function KCNA5 Variants in Pulmonary Arterial Hypertension;American Journal of Respiratory Cell and Molecular Biology;2023-08

3. Kv1.5 channels are regulated by PKC-mediated endocytic degradation;Journal of Biological Chemistry;2021-01

4. Potassium Channels in the Vascular Diseases;Vascular Biology - Selection of Mechanisms and Clinical Applications;2020-11-11

5. Mechanical stretch increases Kv1.5 current through an interaction between the S1–S2 linker and N-terminus of the channel;Journal of Biological Chemistry;2020-04
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