Publication

Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes

Alvarenga Fernandes Sin, O. & Nollen, E. A. A., Nov-2015, In : Cellular and molecular life sciences. 72, 21, p. 4027-4047 21 p.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Alvarenga Fernandes Sin, O., & Nollen, E. A. A. (2015). Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes. Cellular and molecular life sciences, 72(21), 4027-4047. https://doi.org/10.1007/s00018-015-1985-0

Author

Alvarenga Fernandes Sin, Olga ; Nollen, Ellen A. A. / Regulation of protein homeostasis in neurodegenerative diseases : the role of coding and non-coding genes. In: Cellular and molecular life sciences. 2015 ; Vol. 72, No. 21. pp. 4027-4047.

Harvard

Alvarenga Fernandes Sin, O & Nollen, EAA 2015, 'Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes', Cellular and molecular life sciences, vol. 72, no. 21, pp. 4027-4047. https://doi.org/10.1007/s00018-015-1985-0

Standard

Regulation of protein homeostasis in neurodegenerative diseases : the role of coding and non-coding genes. / Alvarenga Fernandes Sin, Olga; Nollen, Ellen A. A.

In: Cellular and molecular life sciences, Vol. 72, No. 21, 11.2015, p. 4027-4047.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Alvarenga Fernandes Sin O, Nollen EAA. Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes. Cellular and molecular life sciences. 2015 Nov;72(21):4027-4047. https://doi.org/10.1007/s00018-015-1985-0


BibTeX

@article{e19516d42bb548b7adcea8314266eb3f,
title = "Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes",
abstract = "Protein homeostasis is fundamental for cell function and survival, because proteins are involved in all aspects of cellular function, ranging from cell metabolism and cell division to the cell's response to environmental challenges. Protein homeostasis is tightly regulated by the synthesis, folding, trafficking and clearance of proteins, all of which act in an orchestrated manner to ensure proteome stability. The protein quality control system is enhanced by stress response pathways, which take action whenever the proteome is challenged by environmental or physiological stress. Aging, however, damages the proteome, and such proteome damage is thought to be associated with aging-related diseases. In this review, we discuss the different cellular processes that define the protein quality control system and focus on their role in protein conformational diseases. We highlight the power of using small organisms to model neurodegenerative diseases and how these models can be exploited to discover genetic modulators of protein aggregation and toxicity. We also link findings from small model organisms to the situation in higher organisms and describe how some of the genetic modifiers discovered in organisms such as worms are functionally conserved throughout evolution. Finally, we demonstrate that the non-coding genome also plays a role in maintaining protein homeostasis. In all, this review highlights the importance of protein and RNA homeostasis in neurodegenerative diseases.",
keywords = "Protein homeostasis, Genetic modifiers, Non-coding RNA, Protein aggregation, Neurodegeneration, Alzheimer's disease, Parkinson's disease, Huntington's disease, C. elegans, Proteotoxicity, Protein quality control, Proteostasis, tRNA, iPOD, JunQ, Aggresome, Chaperone, miRNA, CENTRAL-NERVOUS-SYSTEM, CHAPERONE-MEDIATED AUTOPHAGY, RETICULUM-ASSOCIATED DEGRADATION, NUCLEOTIDE EXCHANGE FACTOR, ER-ASSOCIATED DEGRADATION, AMYLOID FIBRIL FORMATION, ALPHA-SYNUCLEIN BIOLOGY, HEAT-SHOCK RESPONSE, AGE-RELATED DECLINE, ENDOPLASMIC-RETICULUM",
author = "{Alvarenga Fernandes Sin}, Olga and Nollen, {Ellen A. A.}",
year = "2015",
month = "11",
doi = "10.1007/s00018-015-1985-0",
language = "English",
volume = "72",
pages = "4027--4047",
journal = "Cellular and molecular life sciences",
issn = "1420-9071",
publisher = "SPRINGER BASEL AG",
number = "21",

}

RIS

TY - JOUR

T1 - Regulation of protein homeostasis in neurodegenerative diseases

T2 - the role of coding and non-coding genes

AU - Alvarenga Fernandes Sin, Olga

AU - Nollen, Ellen A. A.

PY - 2015/11

Y1 - 2015/11

N2 - Protein homeostasis is fundamental for cell function and survival, because proteins are involved in all aspects of cellular function, ranging from cell metabolism and cell division to the cell's response to environmental challenges. Protein homeostasis is tightly regulated by the synthesis, folding, trafficking and clearance of proteins, all of which act in an orchestrated manner to ensure proteome stability. The protein quality control system is enhanced by stress response pathways, which take action whenever the proteome is challenged by environmental or physiological stress. Aging, however, damages the proteome, and such proteome damage is thought to be associated with aging-related diseases. In this review, we discuss the different cellular processes that define the protein quality control system and focus on their role in protein conformational diseases. We highlight the power of using small organisms to model neurodegenerative diseases and how these models can be exploited to discover genetic modulators of protein aggregation and toxicity. We also link findings from small model organisms to the situation in higher organisms and describe how some of the genetic modifiers discovered in organisms such as worms are functionally conserved throughout evolution. Finally, we demonstrate that the non-coding genome also plays a role in maintaining protein homeostasis. In all, this review highlights the importance of protein and RNA homeostasis in neurodegenerative diseases.

AB - Protein homeostasis is fundamental for cell function and survival, because proteins are involved in all aspects of cellular function, ranging from cell metabolism and cell division to the cell's response to environmental challenges. Protein homeostasis is tightly regulated by the synthesis, folding, trafficking and clearance of proteins, all of which act in an orchestrated manner to ensure proteome stability. The protein quality control system is enhanced by stress response pathways, which take action whenever the proteome is challenged by environmental or physiological stress. Aging, however, damages the proteome, and such proteome damage is thought to be associated with aging-related diseases. In this review, we discuss the different cellular processes that define the protein quality control system and focus on their role in protein conformational diseases. We highlight the power of using small organisms to model neurodegenerative diseases and how these models can be exploited to discover genetic modulators of protein aggregation and toxicity. We also link findings from small model organisms to the situation in higher organisms and describe how some of the genetic modifiers discovered in organisms such as worms are functionally conserved throughout evolution. Finally, we demonstrate that the non-coding genome also plays a role in maintaining protein homeostasis. In all, this review highlights the importance of protein and RNA homeostasis in neurodegenerative diseases.

KW - Protein homeostasis

KW - Genetic modifiers

KW - Non-coding RNA

KW - Protein aggregation

KW - Neurodegeneration

KW - Alzheimer's disease

KW - Parkinson's disease

KW - Huntington's disease

KW - C. elegans

KW - Proteotoxicity

KW - Protein quality control

KW - Proteostasis

KW - tRNA

KW - iPOD

KW - JunQ

KW - Aggresome

KW - Chaperone

KW - miRNA

KW - CENTRAL-NERVOUS-SYSTEM

KW - CHAPERONE-MEDIATED AUTOPHAGY

KW - RETICULUM-ASSOCIATED DEGRADATION

KW - NUCLEOTIDE EXCHANGE FACTOR

KW - ER-ASSOCIATED DEGRADATION

KW - AMYLOID FIBRIL FORMATION

KW - ALPHA-SYNUCLEIN BIOLOGY

KW - HEAT-SHOCK RESPONSE

KW - AGE-RELATED DECLINE

KW - ENDOPLASMIC-RETICULUM

U2 - 10.1007/s00018-015-1985-0

DO - 10.1007/s00018-015-1985-0

M3 - Review article

VL - 72

SP - 4027

EP - 4047

JO - Cellular and molecular life sciences

JF - Cellular and molecular life sciences

SN - 1420-9071

IS - 21

ER -

ID: 25548450