کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10754941 | 1050361 | 2014 | 18 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
IKK regulates the deubiquitinase CYLD at the postsynaptic density
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کلمات کلیدی
NF-κBPSDCaMKIIIKKDeubiquitinaseDUBCa2+/calmodulin-dependent protein kinase II - Ca2 + / calmodulin وابسته پروتئین کیناز IIInhibitor of κB kinase - بازدارنده kB kinasepostsynaptic density - تراکم PostinapticCyld - سیلدnuclear factor κB - فاکتور هسته ای κBElectron microscopy - میکروسکوپ الکترونیUbiquitin - یوبیکویتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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![عکس صفحه اول مقاله: IKK regulates the deubiquitinase CYLD at the postsynaptic density IKK regulates the deubiquitinase CYLD at the postsynaptic density](/preview/png/10754941.png)
چکیده انگلیسی
K63-linked polyubiquitination of proteins regulates their trafficking into specific cellular pathways such as endocytosis and autophagy. CYLD, a deubiquitinase specific for K63-linked polyubiquitins, is present in high quantities at the postsynaptic density (PSD). It was previously shown that, under excitatory conditions, CaMKII activates CYLD in a Ca2+-dependent manner. The observation that CYLD can also be phosphorylated in the absence of Ca2+ in isolated PSDs led us to further explore the regulation of CYLD under basal conditions. A possible involvement of the autonomous form of CaMKII and IKK, both kinases known to be localized at the PSD, was examined. A CaMKII inhibitor CN21 had no effect on CYLD phosphorylation in the absence of Ca2+, but two different IKK inhibitors, IKK16 and tatNEMO, inhibited its phosphorylation. Immuno-electron microscopy on hippocampal cultures, using an antibody for CYLD phosphorylated at S-418, revealed that the phosphorylated form of CYLD is present at the PSD under basal conditions. Phosphorylation of CYLD under basal conditions was inhibited by IKK16. NMDA treatment further promoted phosphorylation of CYLD at the PSD, but IKK16 failed to block the NMDA-induced effect. In vitro experiments using purified proteins demonstrated direct phosphorylation and activation of CYLD by the beta catalytic subunit of IKK. Activation of IKK in isolated PSDs also promoted phosphorylation of CYLD and an increase in endogenous deubiquitinase activity for K63-linked polyubiquitins. Altogether, the results suggest that in the absence of excitatory conditions, constitutive IKK activity at the PSD regulates CYLD and maintains basal levels of K63-linkage specific deubiquitination at the synapse.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 450, Issue 1, 18 July 2014, Pages 550-554
Journal: Biochemical and Biophysical Research Communications - Volume 450, Issue 1, 18 July 2014, Pages 550-554
نویسندگان
Soe Thein, Anna Pham, K. Ulrich Bayer, Jung-Hwa Tao-Cheng, Ayse Dosemeci,