Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and CRL4DCAF5 ubiquitin ligase

Feng Leng; Jiekai Yu; Chunxiao Zhang; Salvador Alejo; Nam Hoang; Hong Sun; Fei Lu; Hui Zhang

doi:10.1038/s41467-018-04019-9

Nature Communications (Apr 2018)

Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and CRL4DCAF5 ubiquitin ligase

Feng Leng,
Jiekai Yu,
Chunxiao Zhang,
Salvador Alejo,
Nam Hoang,
Hong Sun,
Fei Lu,
Hui Zhang

Affiliations

Feng Leng: Department of Chemistry and Biochemistry, University of Nevada
Jiekai Yu: Department of Chemistry and Biochemistry, University of Nevada
Chunxiao Zhang: Department of Chemistry and Biochemistry, University of Nevada
Salvador Alejo: Department of Chemistry and Biochemistry, University of Nevada
Nam Hoang: Department of Chemistry and Biochemistry, University of Nevada
Hong Sun: Department of Chemistry and Biochemistry, University of Nevada
Fei Lu: School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School
Hui Zhang: Department of Chemistry and Biochemistry, University of Nevada

DOI: https://doi.org/10.1038/s41467-018-04019-9
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 17

Abstract

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Lysine methylation is increasingly being implicated in the modification of non-histone proteins. Here the authors find that the methylation of DNMT1 and E2F1 are recognized by the protein L3MBTL3 and the ubiquitin E3 ligase CRL4D C A F5, which cooperatively target these methylated proteins for ubiquitin-dependent proteolysis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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