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10.1073/pnas.1810719115

http://scihub22266oqcxt.onion/10.1073/pnas.1810719115
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C6126765!6126765!30108148
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suck abstract from ncbi


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pmid30108148      Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (35): E8201-10
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  • Structure of the mammalian TRPM7, a magnesium channel required during embryonic development #MMPMID30108148
  • Duan J; Li Z; Li J; Hulse RE; Santa-Cruz A; Valinsky WC; Abiria SA; Krapivinsky G; Zhang J; Clapham DE
  • Proc Natl Acad Sci U S A 2018[Aug]; 115 (35): E8201-10 PMID30108148show ga
  • Ion channels are pore-forming proteins spanning biological membranes. Transient receptor potential ion channels are a subclass of ion channel proteins, characterized by nonselective permeability to cations such as sodium, calcium, magnesium, and zinc, and little voltage sensitivity; their gating is still an area of active investigation. TRPM6 and TRPM7 are ubiquitously expressed with prominent roles in early embryonic development. Uniquely, these channels also include an active kinase domain. The functions of TRPM6 and TRPM7 are correlated with proteolytic cleavage of the kinase domain, which is then translocated to the nucleus to phosphorylate histones and regulate gene expression. Here we describe the structure of the TRPM7 transmembrane regions and compare its features to other ion channels.
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