CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells

Magnesium is essential for cellular life, but how it is homeostatically controlled still remains poorly understood. Here, we report that members of CNNM family, which have been controversially implicated in both cellular Mg 2+ influx and efflux, selectively bind to the TRPM7 channel to stimulate div...

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Vydané v:	PLoS biology Ročník 19; číslo 12; s. e3001496
Hlavní autori:	Bai, Zhiyong, Feng, Jianlin, Franken, Gijs A. C., Al’Saadi, Namariq, Cai, Na, Yu, Albert S., Lou, Liping, Komiya, Yuko, Hoenderop, Joost G. J., de Baaij, Jeroen H. F., Yue, Lixia, Runnels, Loren W.
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States Public Library of Science 20.12.2021 Public Library of Science (PLoS)
Predmet:	Analysis Biology and Life Sciences Cancer Cation Transport Proteins - metabolism Cation Transport Proteins - physiology Cations Cations, Divalent - metabolism Cell Line, Tumor Cell surface Cyclins - metabolism Cyclins - physiology Divalent cations Efflux Experiments Gene expression HEK293 Cells Homeostasis Humans Identification and classification Ion channels Kinases Magnesium Magnesium - metabolism Mass spectrometry Medicine and Health Sciences Membrane proteins Mutation Patch-Clamp Techniques Physical Sciences Physiology Properties Protein expression Protein Serine-Threonine Kinases - metabolism Protein Serine-Threonine Kinases - physiology Proteins Research and Analysis Methods Scientific imaging Short Reports Transient receptor potential proteins TRPM Cation Channels - genetics TRPM Cation Channels - metabolism TRPM Cation Channels - physiology United States Netherlands Iraq
ISSN:	1545-7885, 1544-9173, 1545-7885
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