On July 31, 2021, Zhang, Yu; Liu, Jia; Yu, Dandan; Zhu, Xinxin; Liu, Xiaoyan; Liao, Jun; Li, Sheng; Wang, Huayi published an article.SDS of cas: 79642-50-5 The title of the article was The MLKL kinase-like domain dimerization is an indispensable step of mammalian MLKL activation in necroptosis signaling. And the article contained the following:
MLKL phosphorylation by RIP3 is the commitment step of necroptosis execution, which could induce MLKL activation featured as MLKL monomer-oligomer transition. Here, we reported that the dimerization of the MLKL kinase-like domain was the direct consequence of RIP3 triggered MLKL-phosphorylation. Two inter-dimer interfaces were found in the crystal structure of human MLKL. Mutations destroying both interfaces could prevent RIP3-induced MLKL oligomerization and necroptosis efficiently. Moreover, we confirmed MLKL self-assembly by the internal coiled-coil region is necessary for MLKL oligomerization and function. The mutations disrupting coiled-coil self-assembly repressed necroptosis, but it did not prevent RIP3-induced dimerization of the MLKL kinase-like domain. So that, MLKL activation is a sequential process, which begins with kinase-like domain dimerization, and followed by internal coiled-coil region self-assembly to form a proper MLKL oligomer. Besides human MLKL, structural and functional anal. showed the kinase-like domain dimerization was conserved among mammalian species, suggesting it is a general step of the RIP3-induced MLKL activation process. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).SDS of cas: 79642-50-5
The Article related to mlkl domain dimerization necroptosis signaling, Mammalian Biochemistry: Development and Aging and other aspects.SDS of cas: 79642-50-5
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