Publication

DNAJs: more than substrate delivery to HSPA

Dekker, S. L., Kampinga, H. H. & Bergink, S., 30-Jun-2015, In : Frontiers in Molecular Biosciences. 2, 8 p., 35.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Dekker, S. L., Kampinga, H. H., & Bergink, S. (2015). DNAJs: more than substrate delivery to HSPA. Frontiers in Molecular Biosciences, 2, [35]. https://doi.org/10.3389/fmolb.2015.00035

Author

Dekker, Suzanne L ; Kampinga, Harm H ; Bergink, Steven. / DNAJs : more than substrate delivery to HSPA. In: Frontiers in Molecular Biosciences. 2015 ; Vol. 2.

Harvard

Dekker, SL, Kampinga, HH & Bergink, S 2015, 'DNAJs: more than substrate delivery to HSPA', Frontiers in Molecular Biosciences, vol. 2, 35. https://doi.org/10.3389/fmolb.2015.00035

Standard

DNAJs : more than substrate delivery to HSPA. / Dekker, Suzanne L; Kampinga, Harm H; Bergink, Steven.

In: Frontiers in Molecular Biosciences, Vol. 2, 35, 30.06.2015.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Frontiers in Molecular Biosciences. 2015 Jun 30;2. 35. https://doi.org/10.3389/fmolb.2015.00035


BibTeX

@article{444f4bd8942a49b09ef77aad9859b6f3,
title = "DNAJs: more than substrate delivery to HSPA",
abstract = "Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes can alter this fold and result in misfolding of proteins or even aggregation. Cells are equipped with several pathways that can deal with protein stress. Together, these pathways are referred to as the protein quality control network. The network comprises degradation and (re)folding pathways that are intertwined due to the sharing of components and by the overlap in affinity for substrates. Here, we will give examples of this sharing and intertwinement of protein degradation and protein folding and discuss how the fate of a substrate is determined. We will focus on the ubiquitylation of substrates and the role of Hsp70 co-chaperones of the DNAJ class in this process.",
author = "Dekker, {Suzanne L} and Kampinga, {Harm H} and Steven Bergink",
year = "2015",
month = jun,
day = "30",
doi = "10.3389/fmolb.2015.00035",
language = "English",
volume = "2",
journal = "Frontiers in Molecular Biosciences",
issn = "2296-889X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - DNAJs

T2 - more than substrate delivery to HSPA

AU - Dekker, Suzanne L

AU - Kampinga, Harm H

AU - Bergink, Steven

PY - 2015/6/30

Y1 - 2015/6/30

N2 - Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes can alter this fold and result in misfolding of proteins or even aggregation. Cells are equipped with several pathways that can deal with protein stress. Together, these pathways are referred to as the protein quality control network. The network comprises degradation and (re)folding pathways that are intertwined due to the sharing of components and by the overlap in affinity for substrates. Here, we will give examples of this sharing and intertwinement of protein degradation and protein folding and discuss how the fate of a substrate is determined. We will focus on the ubiquitylation of substrates and the role of Hsp70 co-chaperones of the DNAJ class in this process.

AB - Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes can alter this fold and result in misfolding of proteins or even aggregation. Cells are equipped with several pathways that can deal with protein stress. Together, these pathways are referred to as the protein quality control network. The network comprises degradation and (re)folding pathways that are intertwined due to the sharing of components and by the overlap in affinity for substrates. Here, we will give examples of this sharing and intertwinement of protein degradation and protein folding and discuss how the fate of a substrate is determined. We will focus on the ubiquitylation of substrates and the role of Hsp70 co-chaperones of the DNAJ class in this process.

U2 - 10.3389/fmolb.2015.00035

DO - 10.3389/fmolb.2015.00035

M3 - Article

C2 - 26176011

VL - 2

JO - Frontiers in Molecular Biosciences

JF - Frontiers in Molecular Biosciences

SN - 2296-889X

M1 - 35

ER -

ID: 21973388