COMMD1 (Copper Metabolism MURR1 Domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding

Xicheng Mao, Nathan Gluck, Baozhi Chen, Petro Starokadomskyy, Haiying Li, Gabriel N. Maine, Ezra Burstein

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.

Original languageEnglish (US)
Pages (from-to)32355-32365
Number of pages11
JournalJournal of Biological Chemistry
Volume286
Issue number37
DOIs
StatePublished - Sep 16 2011

Fingerprint

Cullin Proteins
Ligases
Protein Binding
Metabolism
Copper
Proteins
Cullin 1
Protein Domains
Chemical activation
Substrates
Ubiquitination
Ubiquitin

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

COMMD1 (Copper Metabolism MURR1 Domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding. / Mao, Xicheng; Gluck, Nathan; Chen, Baozhi; Starokadomskyy, Petro; Li, Haiying; Maine, Gabriel N.; Burstein, Ezra.

In: Journal of Biological Chemistry, Vol. 286, No. 37, 16.09.2011, p. 32355-32365.

Research output: Contribution to journalArticle

Mao, Xicheng ; Gluck, Nathan ; Chen, Baozhi ; Starokadomskyy, Petro ; Li, Haiying ; Maine, Gabriel N. ; Burstein, Ezra. / COMMD1 (Copper Metabolism MURR1 Domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding. In: Journal of Biological Chemistry. 2011 ; Vol. 286, No. 37. pp. 32355-32365.
@article{5de2e0a7f0e24cf5b63648df601334d0,
title = "COMMD1 (Copper Metabolism MURR1 Domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding",
abstract = "Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.",
author = "Xicheng Mao and Nathan Gluck and Baozhi Chen and Petro Starokadomskyy and Haiying Li and Maine, {Gabriel N.} and Ezra Burstein",
year = "2011",
month = "9",
day = "16",
doi = "10.1074/jbc.M111.278408",
language = "English (US)",
volume = "286",
pages = "32355--32365",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "37",

}

TY - JOUR

T1 - COMMD1 (Copper Metabolism MURR1 Domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding

AU - Mao, Xicheng

AU - Gluck, Nathan

AU - Chen, Baozhi

AU - Starokadomskyy, Petro

AU - Li, Haiying

AU - Maine, Gabriel N.

AU - Burstein, Ezra

PY - 2011/9/16

Y1 - 2011/9/16

N2 - Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.

AB - Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.

UR - http://www.scopus.com/inward/record.url?scp=80052721462&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052721462&partnerID=8YFLogxK

U2 - 10.1074/jbc.M111.278408

DO - 10.1074/jbc.M111.278408

M3 - Article

C2 - 21778237

AN - SCOPUS:80052721462

VL - 286

SP - 32355

EP - 32365

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 37

ER -