An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells

Michael Ohh; William Y. Kim; Javid J. Moslehi; Yuzhi Chen; Vincent Chau; Margaret A. Read; William G. Kaelin

doi:10.1093/embo-reports/kvf028

An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells

Michael Ohh, William Y. Kim, Javid J. Moslehi, Yuzhi Chen, Vincent Chau, Margaret A. Read, William G. Kaelin

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160 Scopus citations

Abstract

Skp1-Cdc53/Cul1-F-box (SCF) complexes constitute a class of E3 ubiquitin ligases. Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes. Cdc53 and the Cullins can become covalently linked to the ubiquitin-like molecule Rub1/NEDD8. Inhibition of neddylation inhibits SCF function in vitro and in yeast and plants. Here we show that ongoing neddylation is likewise required for VEC function in vitro and for the degradation of SCF and VEC targets in mammalian cells. Thus, neddylation regulates the activity of two specific subclasses of mammalian ubiquitin ligases.

Original language	English (US)
Pages (from-to)	177-182
Number of pages	6
Journal	EMBO Reports
Volume	3
Issue number	2
DOIs	https://doi.org/10.1093/embo-reports/kvf028
State	Published - Jan 1 2002

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Genetics

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abstract = "Skp1-Cdc53/Cul1-F-box (SCF) complexes constitute a class of E3 ubiquitin ligases. Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes. Cdc53 and the Cullins can become covalently linked to the ubiquitin-like molecule Rub1/NEDD8. Inhibition of neddylation inhibits SCF function in vitro and in yeast and plants. Here we show that ongoing neddylation is likewise required for VEC function in vitro and for the degradation of SCF and VEC targets in mammalian cells. Thus, neddylation regulates the activity of two specific subclasses of mammalian ubiquitin ligases.",

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T1 - An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells

AU - Ohh, Michael

AU - Kim, William Y.

AU - Moslehi, Javid J.

AU - Chen, Yuzhi

AU - Chau, Vincent

AU - Read, Margaret A.

AU - Kaelin, William G.

PY - 2002/1/1

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AB - Skp1-Cdc53/Cul1-F-box (SCF) complexes constitute a class of E3 ubiquitin ligases. Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes. Cdc53 and the Cullins can become covalently linked to the ubiquitin-like molecule Rub1/NEDD8. Inhibition of neddylation inhibits SCF function in vitro and in yeast and plants. Here we show that ongoing neddylation is likewise required for VEC function in vitro and for the degradation of SCF and VEC targets in mammalian cells. Thus, neddylation regulates the activity of two specific subclasses of mammalian ubiquitin ligases.

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An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells

Abstract

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