In:
Journal of Cellular Biochemistry, Wiley, Vol. 122, No. 3-4 ( 2021-04), p. 326-334
Abstract:
The Skp1‐Cul1‐F‐box protein (SCF) E3 ligase complex is one of the largest ubiquitin E3 ligase families. FBXL19, a F‐box protein in SCF FBXL19 E3 ligase complex, regulates a variety of cellular responses including cell migration. We have shown that FBXL19 is not stable and its degradation is mediated by the ubiquitin–proteasome system, while the ubiquitin E3 ligase for FBXL19 ubiquitination and degradation has not been identified. In the study, we discovered that a new ubiquitin E3 ligase, SCF FBXW17 , ubiquitinates and induces FBXL19 degradation. Exogenous FBXW17 targets FBXL19 for its ubiquitination and degradation. Lysine 114 in FBXL19 is a potential ubiquitin acceptor site. Acetylation of FBXL19 attenuated SCF FBXW17 ‐mediated FBXL19 degradation. SCF FBXL19 E3 ligase reduced Rac1 levels and cell migration, while the effects were attenuated by exogenous FBXW17. Downregulation of FBXW17 attenuated lysophosphatidic acid‐induced lamellipodia formation and Rac1 accumulation at migration leading edge. Taken together with our previous studies, FBXL19 is degraded by the ubiquitin–proteasome system and its site‐specific ubiquitination is mediated by SCF FBXW17 E3 ligase, which promotes cell migration.
Type of Medium:
Online Resource
ISSN:
0730-2312
,
1097-4644
DOI:
10.1002/jcb.v122.3-4
Language:
English
Publisher:
Wiley
Publication Date:
2021
detail.hit.zdb_id:
1479976-5
SSG:
12
