Substrate Phosphorylation and Feedback Regulation in JFK-promoted p53 Destabilization
نویسندگان
چکیده
منابع مشابه
Mechanism of feedback regulation of insulin receptor substrate-1 phosphorylation in primary adipocytes.
Serine and threonine phosphorylation of IRS-1 (insulin receptor substrate-1) has been reported to decrease its ability to be tyrosine-phosphorylated by the insulin receptor. Insulin itself may negatively regulate tyrosine phosphorylation of IRS-1 through a PI3K (phosphoinositide 3-kinase)-dependent feedback pathway. In the present study, we examined the regulation and role of IRS-1 serine phosp...
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The p53 tumor suppressor plays a central role in integrating cellular responses to various stresses. Tight regulation of p53 is thus essential for the maintenance of genome integrity and normal cell proliferation. Currently, several ubiquitin ligases, including the single-subunit RING-finger types--MDM2, Pirh2, and COP1--and the HECT-domain type--ARF-BP1--have been reported to target p53 for de...
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In this paper we investigate the robustness of stability of linear systems _ x = Ax resp. x(t + 1) = Ax(t) under complex or real (i) time-varying linear, (ii) nonlinear, (iii) time-varying nonlinear, or (iv) dynamic parameter perturbations of the output feedback type. The class of dynamic perturbations is suuciently wide to account for all kinds of neglected dynamics with nite gain encountered ...
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The tumor suppressor wild-type p53 can induce apoptosis. M1-t-p53 myeloid leukemic cells have a temperature-sensitive p53 protein that changes its conformation to wild-type p53 after transfer from 37 degrees C to 32 degrees C. We have now found that these cells showed an early lysosomal rupture after transfer to 32 degrees C. Mitochondrial damage, including decreased membrane potential and rele...
متن کاملReciprocal feedback regulation of insulin receptor and insulin receptor substrate tyrosine phosphorylation by phosphoinositide 3-kinase in primary adipocytes.
Signalling by the insulin receptor substrate (IRS) proteins is critically dependent on the tyrosine phosphorylation of specific binding sites that recruit Src homology 2 (SH2)-domain-containing proteins, such as the p85 subunit of phosphoinositide 3-kinase (PI 3-kinase), the tyrosine phosphatase SHP-2 and the adapter protein Grb2. Here we show that stimulation by insulin of freshly isolated pri...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.195115