Publication

The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner

Vonk, W. I. M., Kakkar, V., Bartuzi, P., Jaarsma, D., Berger, R., Hofker, M. H., Klomp, L. W. J., Wijmenga, C., Kampinga, H. H. & van de Sluis, B., 1-Apr-2014, In : PLoS ONE. 9, 4, 13 p., e92408.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Vonk, W. I. M., Kakkar, V., Bartuzi, P., Jaarsma, D., Berger, R., Hofker, M. H., Klomp, L. W. J., Wijmenga, C., Kampinga, H. H., & van de Sluis, B. (2014). The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner. PLoS ONE, 9(4), [e92408]. https://doi.org/10.1371/journal.pone.0092408

Author

Vonk, Willianne I. M. ; Kakkar, Vaishali ; Bartuzi, Paulina ; Jaarsma, Dick ; Berger, Ruud ; Hofker, Marten H. ; Klomp, Leo W. J. ; Wijmenga, Cisca ; Kampinga, Harm H. ; van de Sluis, Bart. / The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner. In: PLoS ONE. 2014 ; Vol. 9, No. 4.

Harvard

Vonk, WIM, Kakkar, V, Bartuzi, P, Jaarsma, D, Berger, R, Hofker, MH, Klomp, LWJ, Wijmenga, C, Kampinga, HH & van de Sluis, B 2014, 'The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner', PLoS ONE, vol. 9, no. 4, e92408. https://doi.org/10.1371/journal.pone.0092408

Standard

The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner. / Vonk, Willianne I. M.; Kakkar, Vaishali; Bartuzi, Paulina; Jaarsma, Dick; Berger, Ruud; Hofker, Marten H.; Klomp, Leo W. J.; Wijmenga, Cisca; Kampinga, Harm H.; van de Sluis, Bart.

In: PLoS ONE, Vol. 9, No. 4, e92408, 01.04.2014.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Vonk WIM, Kakkar V, Bartuzi P, Jaarsma D, Berger R, Hofker MH et al. The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner. PLoS ONE. 2014 Apr 1;9(4). e92408. https://doi.org/10.1371/journal.pone.0092408


BibTeX

@article{d43ac837e1bc48bf98359f4581030e05,
title = "The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner",
abstract = "The Copper Metabolism MURR1 domain protein 1 (COMMD1) is a protein involved in multiple cellular pathways, including copper homeostasis, NF-kappa B and hypoxia signalling. Acting as a scaffold protein, COMMD1 mediates the levels, stability and proteolysis of its substrates (e.g. the copper-transporters ATP7B and ATP7A, RELA and HIF-1 alpha). Recently, we established an interaction between the Cu/Zn superoxide dismutase 1 (SOD1) and COMMD1, resulting in a decreased maturation and activation of SOD1. Mutations in SOD1, associated with the progressive neurodegenerative disorder Amyotrophic Lateral Sclerosis (ALS), cause misfolding and aggregation of the mutant SOD1 (mSOD1) protein. Here, we identify COMMD1 as a novel regulator of misfolded protein aggregation as it enhances the formation of mSOD1 aggregates upon binding. Interestingly, COMMD1 co-localizes to the sites of mSOD1 inclusions and forms high molecular weight complexes in the presence of mSOD1. The effect of COMMD1 on protein aggregation is client-specific as, in contrast to mSOD1, COMMD1 decreases the abundance of mutant Parkin inclusions, associated with Parkinson's disease. Aggregation of a polyglutamine-expanded Huntingtin, causative of Huntington's disease, appears unaltered by COMMD1. Altogether, this study offers new research directions to expand our current knowledge on the mechanisms underlying aggregation disease pathologies.",
keywords = "AMYOTROPHIC-LATERAL-SCLEROSIS, MOTOR-NEURON DISEASE, SUPEROXIDE-DISMUTASE SOD1, EPITHELIAL SODIUM-CHANNEL, MUTANT SOD1, CU,ZN-SUPEROXIDE DISMUTASE, HUNTINGTONS-DISEASE, PARKINSONS-DISEASE, FAMILIAL ALS, IN-VIVO",
author = "Vonk, {Willianne I. M.} and Vaishali Kakkar and Paulina Bartuzi and Dick Jaarsma and Ruud Berger and Hofker, {Marten H.} and Klomp, {Leo W. J.} and Cisca Wijmenga and Kampinga, {Harm H.} and {van de Sluis}, Bart",
year = "2014",
month = apr,
day = "1",
doi = "10.1371/journal.pone.0092408",
language = "English",
volume = "9",
journal = "PLOS-One",
issn = "1932-6203",
publisher = "PUBLIC LIBRARY SCIENCE",
number = "4",

}

RIS

TY - JOUR

T1 - The Copper Metabolism MURR1 Domain Protein 1 (COMMD1) Modulates the Aggregation of Misfolded Protein Species in a Client-Specific Manner

AU - Vonk, Willianne I. M.

AU - Kakkar, Vaishali

AU - Bartuzi, Paulina

AU - Jaarsma, Dick

AU - Berger, Ruud

AU - Hofker, Marten H.

AU - Klomp, Leo W. J.

AU - Wijmenga, Cisca

AU - Kampinga, Harm H.

AU - van de Sluis, Bart

PY - 2014/4/1

Y1 - 2014/4/1

N2 - The Copper Metabolism MURR1 domain protein 1 (COMMD1) is a protein involved in multiple cellular pathways, including copper homeostasis, NF-kappa B and hypoxia signalling. Acting as a scaffold protein, COMMD1 mediates the levels, stability and proteolysis of its substrates (e.g. the copper-transporters ATP7B and ATP7A, RELA and HIF-1 alpha). Recently, we established an interaction between the Cu/Zn superoxide dismutase 1 (SOD1) and COMMD1, resulting in a decreased maturation and activation of SOD1. Mutations in SOD1, associated with the progressive neurodegenerative disorder Amyotrophic Lateral Sclerosis (ALS), cause misfolding and aggregation of the mutant SOD1 (mSOD1) protein. Here, we identify COMMD1 as a novel regulator of misfolded protein aggregation as it enhances the formation of mSOD1 aggregates upon binding. Interestingly, COMMD1 co-localizes to the sites of mSOD1 inclusions and forms high molecular weight complexes in the presence of mSOD1. The effect of COMMD1 on protein aggregation is client-specific as, in contrast to mSOD1, COMMD1 decreases the abundance of mutant Parkin inclusions, associated with Parkinson's disease. Aggregation of a polyglutamine-expanded Huntingtin, causative of Huntington's disease, appears unaltered by COMMD1. Altogether, this study offers new research directions to expand our current knowledge on the mechanisms underlying aggregation disease pathologies.

AB - The Copper Metabolism MURR1 domain protein 1 (COMMD1) is a protein involved in multiple cellular pathways, including copper homeostasis, NF-kappa B and hypoxia signalling. Acting as a scaffold protein, COMMD1 mediates the levels, stability and proteolysis of its substrates (e.g. the copper-transporters ATP7B and ATP7A, RELA and HIF-1 alpha). Recently, we established an interaction between the Cu/Zn superoxide dismutase 1 (SOD1) and COMMD1, resulting in a decreased maturation and activation of SOD1. Mutations in SOD1, associated with the progressive neurodegenerative disorder Amyotrophic Lateral Sclerosis (ALS), cause misfolding and aggregation of the mutant SOD1 (mSOD1) protein. Here, we identify COMMD1 as a novel regulator of misfolded protein aggregation as it enhances the formation of mSOD1 aggregates upon binding. Interestingly, COMMD1 co-localizes to the sites of mSOD1 inclusions and forms high molecular weight complexes in the presence of mSOD1. The effect of COMMD1 on protein aggregation is client-specific as, in contrast to mSOD1, COMMD1 decreases the abundance of mutant Parkin inclusions, associated with Parkinson's disease. Aggregation of a polyglutamine-expanded Huntingtin, causative of Huntington's disease, appears unaltered by COMMD1. Altogether, this study offers new research directions to expand our current knowledge on the mechanisms underlying aggregation disease pathologies.

KW - AMYOTROPHIC-LATERAL-SCLEROSIS

KW - MOTOR-NEURON DISEASE

KW - SUPEROXIDE-DISMUTASE SOD1

KW - EPITHELIAL SODIUM-CHANNEL

KW - MUTANT SOD1

KW - CU,ZN-SUPEROXIDE DISMUTASE

KW - HUNTINGTONS-DISEASE

KW - PARKINSONS-DISEASE

KW - FAMILIAL ALS

KW - IN-VIVO

U2 - 10.1371/journal.pone.0092408

DO - 10.1371/journal.pone.0092408

M3 - Article

C2 - 24691167

VL - 9

JO - PLOS-One

JF - PLOS-One

SN - 1932-6203

IS - 4

M1 - e92408

ER -

ID: 13998817