| Regulation of Krüpple-like factor 5 by targeted protein degradation. | |
MedLine Citation:
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PMID: 20694673 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Transcription factors are usually unstable proteins. The degradation of the majority of transcription factors is through the ubiquitin proteasome pathway and is tightly regulated by E3 ubiquitin ligases. KLF5 is an important transcription factor regulating cell proliferation, cell cycle, survival, migration, differentiation, angiogenesis, and stem cell self-renewal. We have shown that the WWP1 E3 ligase targets KLF5 for ubiquitin-mediated degradation. Several methods to determine whether a protein is ubiquitinated have been described [Kaiser, Tagwerker (Methods Enzymol 399:243-248, 2005); Bloom, Pagano (Methods Enzymol 399:249-266, 2005)]. This chapter focuses on experimental approaches testing KLF5 transcription factor ubiquitination and degradation by its E3s. |
Authors:
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Ceshi Chen |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Methods in molecular biology (Clifton, N.J.) Volume: 647 ISSN: 1940-6029 ISO Abbreviation: Methods Mol. Biol. Publication Date: 2010 |
Date Detail:
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Created Date: 2010-08-09 Completed Date: 2010-12-28 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9214969 Medline TA: Methods Mol Biol Country: United States |
Other Details:
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Languages: eng Pagination: 267-77 Citation Subset: IM |
Affiliation:
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Center for Cell Biology and Cancer Research, Albany Medical College, Albany, NY, USA. chenc@mail.amc.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Line, Tumor Immunoprecipitation Kruppel-Like Transcription Factors / chemistry, metabolism* Protein Denaturation Ubiquitin-Protein Ligases / metabolism Ubiquitination |
| Chemical | |
Reg. No./Substance:
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0/Kruppel-Like Transcription Factors; EC 6.3.2.19/Ubiquitin-Protein Ligases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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