New ATPase regulators-p97 goes to the PUB

Louise Madsen; Michael Seeger; Colin A Semple; Rasmus Hartmann-Petersen

doi:10.1016/j.biocel.2009.05.017

New ATPase regulators-p97 goes to the PUB

Louise Madsen, Michael Seeger, Colin A Semple, Rasmus Hartmann-Petersen

Biomolecular Sciences

53 Citations (Scopus)

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.

Original language	English
Journal	International Journal of Biochemistry & Cell Biology
Volume	41
Issue number	12
Pages (from-to)	2380-8
Number of pages	8
ISSN	1357-2725
DOIs	https://doi.org/10.1016/j.biocel.2009.05.017
Publication status	Published - 2009

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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.",

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journal = "International Journal of Biochemistry and Cell Biology",

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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

SN - 1357-2725

VL - 41

SP - 2380

EP - 2388

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

IS - 12

ER -

New ATPase regulators-p97 goes to the PUB

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