SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitina...
SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
About this item
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Author / Creator
Luo, Hong-Bin , Xia, Yi-Yuan , Shu, Xi-Ji , Liu, Zan-Chao , Feng, Ye , Liu, Xing-Hua , Yu, Guang , Yin, Gang , Xiong, Yan-Si , Zeng, Kuan , Jiang, Jun , Ye, Keqiang , Wang, Xiao-Chuan and Wang, Jian-Zhi
Publisher
United States: National Academy of Sciences
Journal title
Language
English
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Publication information
Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
Significance Intracellular accumulation of the abnormally modified tau is hallmark pathology of AD, but the mechanism leading to tau aggregation is not fully characterized. In the present study, we studied the effects of tau SUMOylation on its phosphorylation, ubiquitination, degradation, and aggregation. We discovered that sumoylation competes wit...
Alternative Titles
Full title
SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
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Record Identifier
TN_cdi_proquest_journals_1627727457
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1627727457
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1417548111
