NDLI: Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

Content Provider	PubMed Central
Author	Zhang, Qiansen Zhou, Pingzheng Chen, Zhuxi Li, Min Jiang, Hualiang Gao, Zhaobing Yang, Huaiyu
Abstract	Many membrane protein functions require phosphatidylinositol-4,5-bisphosphate (PIP2), a minor phospholipid in the inner leaflet of plasma membranes; however the underlying mechanisms have not been well elucidated. Here, we show that PIP2 might differentially regulate the activities of highly homologous proteins. The voltage-gated potassium (Kv) channels Shaker, Kv1.2 and KCNQ2 have similar structural arrangements and voltage sensing mechanisms. Previous studies showed that PIP2 decreases the voltage sensitivity of the Shaker and Kv1.2 channels; we observed that PIP2 up-regulates the voltage sensitivity of the KCNQ2 channel. The differential interactions of PIP2 with these channels contribute to the diversity of PIP2 regulations. Our data suggest that the effects of PIP2 and its interactions with membrane proteins should be studied at a finer scale.
Related Links	http://dx.doi.org/10.1073/pnas.1312483110
Ending Page	20098
Page Count	6
Starting Page	20093
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	50
Volume Number	110
Language	English
Publisher	National Academy of Sciences
Publisher Date	2013-12-10
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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