Abstract:
:Transient receptor potential melastatin-like 7 (TRPM7) is a channel protein that also contains a regulatory serine-threonine kinase domain. Here, we find that Trpm7-/- T cells are deficient in Fas-receptor-induced apoptosis and that TRPM7 channel activity participates in the apoptotic process and is regulated by caspase-dependent cleavage. This function of TRPM7 is dependent on its function as a channel, but not as a kinase. TRPM7 is cleaved by caspases at D1510, disassociating the carboxy-terminal kinase domain from the pore without disrupting the phosphotransferase activity of the released kinase but substantially increasing TRPM7 ion channel activity. Furthermore, we show that TRPM7 regulates endocytic compartmentalization of the Fas receptor after receptor stimulation, an important process for apoptotic signaling through Fas receptors. These findings raise the possibility that other members of the TRP channel superfamily are also regulated by caspase-mediated cleavage, with wide-ranging implications for cell death and differentiation.
journal_name
Dev Celljournal_title
Developmental cellauthors
Desai BN,Krapivinsky G,Navarro B,Krapivinsky L,Carter BC,Febvay S,Delling M,Penumaka A,Ramsey IS,Manasian Y,Clapham DEdoi
10.1016/j.devcel.2012.04.006subject
Has Abstractpub_date
2012-06-12 00:00:00pages
1149-62issue
6eissn
1534-5807issn
1878-1551pii
S1534-5807(12)00183-9journal_volume
22pub_type
杂志文章abstract::The E-Cadherin-catenin complex plays a critical role in epithelial cell-cell adhesion, polarization, and morphogenesis. Here, we have analyzed the mechanism of Drosophila E-Cadherin (DE-Cad) localization. Loss of function of the Drosophila exocyst components sec5, sec6, and sec15 in epithelial cells results in DE-Cad ...
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