Inactivation of USP14 Perturbs Ubiquitin Homeostasis and Delays the Cell Cycle in Mouse Embryonic Fibroblasts and in Fruit Fly Drosophila | Zendy

JungHoon Lee | Zendy; Seoyoung Park | Zendy; Yejin Yun | Zendy; Won Hoon Choi | Zendy; Min-Ji Kang | Zendy; Min Jae Lee | Zendy

Open Access

Inactivation of USP14 Perturbs Ubiquitin Homeostasis and Delays the Cell Cycle in Mouse Embryonic Fibroblasts and in Fruit Fly Drosophila

Author(s) -

JungHoon Lee,

Seoyoung Park,

Yejin Yun,

Won Hoon Choi,

Min-Ji Kang,

Min Jae Lee

Publication year - 2018

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000489750

Subject(s) - deubiquitinating enzyme , ubiquitin , proteasome , microbiology and biotechnology , biology , cell cycle , proteases , embryonic stem cell , cell , genetics , biochemistry , enzyme , gene

The 26S proteasome is the key proteolytic complex for recognition and degradation of polyubiquitinated target substrates in eukaryotes. Among numerous proteasome-associated proteins, a deubiquitinating enzyme (DUB) USP14 has been identified as an endogenous inhibitor of the proteasome. Here, we explored the complex regulatory functions of USP14 that involve ubiquitin (Ub) homeostasis and substrate degradation in flies and mammals.

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