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Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes

Overview of attention for article published in BMC Molecular and Cell Biology, May 2008
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Title
Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
Published in
BMC Molecular and Cell Biology, May 2008
DOI 10.1186/1472-6807-8-26
Pubmed ID
Authors

Zhen Xu, Ekta Kohli, Karl I Devlin, Michael Bold, Jay C Nix, Saurav Misra

Abstract

Ubiquitin (E3) ligases interact with specific ubiquitin conjugating (E2) enzymes to ubiquitinate particular substrate proteins. As the combination of E2 and E3 dictates the type and biological consequence of ubiquitination, it is important to understand the basis of specificity in E2:E3 interactions. The E3 ligase CHIP interacts with Hsp70 and Hsp90 and ubiquitinates client proteins that are chaperoned by these heat shock proteins. CHIP interacts with two types of E2 enzymes, UbcH5 and Ubc13-Uev1a. It is unclear, however, why CHIP binds these E2 enzymes rather than others, and whether CHIP interacts preferentially with UbcH5 or Ubc13-Uev1a, which form different types of polyubiquitin chains.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 79 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Chile 1 1%
United States 1 1%
India 1 1%
Germany 1 1%
Unknown 75 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 19 24%
Researcher 9 11%
Student > Bachelor 8 10%
Student > Master 8 10%
Student > Doctoral Student 3 4%
Other 11 14%
Unknown 21 27%
Readers by discipline Count As %
Agricultural and Biological Sciences 27 34%
Biochemistry, Genetics and Molecular Biology 20 25%
Neuroscience 2 3%
Engineering 2 3%
Medicine and Dentistry 2 3%
Other 4 5%
Unknown 22 28%