New ATPase regulators-p97 goes to the PUB

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Standard

New ATPase regulators-p97 goes to the PUB. / Madsen, Louise; Seeger, Michael; Semple, Colin A; Hartmann-Petersen, Rasmus.

I: International Journal of Biochemistry & Cell Biology, Bind 41, Nr. 12, 2009, s. 2380-8.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Madsen, L, Seeger, M, Semple, CA & Hartmann-Petersen, R 2009, 'New ATPase regulators-p97 goes to the PUB', International Journal of Biochemistry & Cell Biology, bind 41, nr. 12, s. 2380-8. https://doi.org/10.1016/j.biocel.2009.05.017

APA

Madsen, L., Seeger, M., Semple, C. A., & Hartmann-Petersen, R. (2009). New ATPase regulators-p97 goes to the PUB. International Journal of Biochemistry & Cell Biology, 41(12), 2380-8. https://doi.org/10.1016/j.biocel.2009.05.017

Vancouver

Madsen L, Seeger M, Semple CA, Hartmann-Petersen R. New ATPase regulators-p97 goes to the PUB. International Journal of Biochemistry & Cell Biology. 2009;41(12):2380-8. https://doi.org/10.1016/j.biocel.2009.05.017

Author

Madsen, Louise ; Seeger, Michael ; Semple, Colin A ; Hartmann-Petersen, Rasmus. / New ATPase regulators-p97 goes to the PUB. I: International Journal of Biochemistry & Cell Biology. 2009 ; Bind 41, Nr. 12. s. 2380-8.

Bibtex

@article{b57d52a0e50511deba73000ea68e967b,
title = "New ATPase regulators-p97 goes to the PUB",
abstract = "The conserved eukaryotic AAA-type ATPase complex, known as p97 or VCP in mammals and Cdc48 in yeast, is involved in a number of cellular pathways, including fusion of homotypic membranes, protein degradation, and activation of membrane-bound transcription factors. Most likely, p97 is directed to this broad spectrum of cellular functions through its binding to specific cofactors. More than 20 different p97 cofactors have been described to date and our understanding of their cellular functions is rapidly expanding. Common to these proteins is their intimate connection with the ubiquitin system. Recently, a small, conserved family of proteins, containing PUB domains, was found to function as p97 adaptors. Intriguingly, their association with p97 is regulated by tyrosine phosphorylation, suggesting that they act as a relay between signalling pathways and p97 functions. Here we give an overview of the currently known PUB-domain proteins and other p97-interacting proteins.",
author = "Louise Madsen and Michael Seeger and Semple, {Colin A} and Rasmus Hartmann-Petersen",
year = "2009",
doi = "10.1016/j.biocel.2009.05.017",
language = "English",
volume = "41",
pages = "2380--8",
journal = "International Journal of Biochemistry & Cell Biology",
issn = "1357-2725",
publisher = "Elsevier",
number = "12",

}

RIS

TY - JOUR

T1 - New ATPase regulators-p97 goes to the PUB

AU - Madsen, Louise

AU - Seeger, Michael

AU - Semple, Colin A

AU - Hartmann-Petersen, Rasmus

PY - 2009

Y1 - 2009

N2 - The conserved eukaryotic AAA-type ATPase complex, known as p97 or VCP in mammals and Cdc48 in yeast, is involved in a number of cellular pathways, including fusion of homotypic membranes, protein degradation, and activation of membrane-bound transcription factors. Most likely, p97 is directed to this broad spectrum of cellular functions through its binding to specific cofactors. More than 20 different p97 cofactors have been described to date and our understanding of their cellular functions is rapidly expanding. Common to these proteins is their intimate connection with the ubiquitin system. Recently, a small, conserved family of proteins, containing PUB domains, was found to function as p97 adaptors. Intriguingly, their association with p97 is regulated by tyrosine phosphorylation, suggesting that they act as a relay between signalling pathways and p97 functions. Here we give an overview of the currently known PUB-domain proteins and other p97-interacting proteins.

AB - The conserved eukaryotic AAA-type ATPase complex, known as p97 or VCP in mammals and Cdc48 in yeast, is involved in a number of cellular pathways, including fusion of homotypic membranes, protein degradation, and activation of membrane-bound transcription factors. Most likely, p97 is directed to this broad spectrum of cellular functions through its binding to specific cofactors. More than 20 different p97 cofactors have been described to date and our understanding of their cellular functions is rapidly expanding. Common to these proteins is their intimate connection with the ubiquitin system. Recently, a small, conserved family of proteins, containing PUB domains, was found to function as p97 adaptors. Intriguingly, their association with p97 is regulated by tyrosine phosphorylation, suggesting that they act as a relay between signalling pathways and p97 functions. Here we give an overview of the currently known PUB-domain proteins and other p97-interacting proteins.

U2 - 10.1016/j.biocel.2009.05.017

DO - 10.1016/j.biocel.2009.05.017

M3 - Journal article

C2 - 19497384

VL - 41

SP - 2380

EP - 2388

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

SN - 1357-2725

IS - 12

ER -

ID: 16187752