The TRPM7 ion channel modifies histones
نویسندگان
چکیده
منابع مشابه
Ion channel-kinase TRPM7 is required for maintaining cardiac automaticity.
Sick sinus syndrome and atrioventricular block are common clinical problems, often necessitating permanent pacemaker placement, yet the pathophysiology of these conditions remains poorly understood. Here we show that Transient Receptor Potential Melastatin 7 (TRPM7), a divalent-permeant channel-kinase of unknown function, is highly expressed in embryonic myocardium and sinoatrial node (SAN) and...
متن کاملThe Pathophysiologic Roles of TRPM7 Channel
Transient receptor potential melastatin 7 (TRPM7) is a member of the melastatin-related subfamily and contains a channel and a kinase domain. TRPM7 is known to be associated with cell proliferation, survival, and development. It is ubiquitously expressed, highly permeable to Mg(2+) and Ca(2+), and its channel activity is negatively regulated by free Mg(2+) and Mg-complexed nucleotides. Recent s...
متن کاملThe TRPM7 Ion Channel Functions in Cholinergic Synaptic Vesicles and Affects Transmitter Release
A longstanding hypothesis is that ion channels are present in the membranes of synaptic vesicles and might affect neurotransmitter release. Here we demonstrate that TRPM7, a member of the transient receptor potential (TRP) ion channel family, resides in the membrane of synaptic vesicles of sympathetic neurons, forms molecular complexes with the synaptic vesicle proteins synapsin I and synaptota...
متن کاملTRPM7 Provides an Ion Channel Mechanism for Cellular Entry of Trace Metal Ions
Trace metal ions such as Zn(2+), Fe(2+), Cu(2+), Mn(2+), and Co(2+) are required cofactors for many essential cellular enzymes, yet little is known about the mechanisms through which they enter into cells. We have shown previously that the widely expressed ion channel TRPM7 (LTRPC7, ChaK1, TRP-PLIK) functions as a Ca(2+)- and Mg(2+)-permeable cation channel, whose activity is regulated by intra...
متن کاملLysine methyltransferase SETD6 modifies histones and non-histone proteins
Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, we report new substrates for the lysine methyltransferase SETD6. Based on the SETD6catalysed site on the histone variant H2AZ, we identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6...
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ژورنال
عنوان ژورنال: Nature Reviews Molecular Cell Biology
سال: 2014
ISSN: 1471-0072,1471-0080
DOI: 10.1038/nrm3824