A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase
p97/VCP (known as Cdc48 in S. cerevisiae or TER94 in Drosophila) is one of the most abundant cytosolic ATPases. It is highly conserved from archaebacteria to eukaryotes. In conjunction with a large number of cofactors and adaptors, it couples ATP hydrolysis to segregation of polypeptides from immobi...
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doaj-03a9c30522cc4d9c9783b93f2503d2772020-11-24T23:47:55ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2017-06-01410.3389/fmolb.2017.00039250527A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPaseYihong Ye0Wai Kwan Tang1Ting Zhang2Di Xia3Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthBethesda, MD, United StatesLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of HealthBethesda, MD, United StatesLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthBethesda, MD, United StatesLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of HealthBethesda, MD, United Statesp97/VCP (known as Cdc48 in S. cerevisiae or TER94 in Drosophila) is one of the most abundant cytosolic ATPases. It is highly conserved from archaebacteria to eukaryotes. In conjunction with a large number of cofactors and adaptors, it couples ATP hydrolysis to segregation of polypeptides from immobile cellular structures such as protein assemblies, membranes, ribosome, and chromatin. This often results in proteasomal degradation of extracted polypeptides. Given the diversity of p97 substrates, this “segregase” activity has profound influence on cellular physiology ranging from protein homeostasis to DNA lesion sensing, and mutations in p97 have been linked to several human diseases. Here we summarize our current understanding of the structure and function of this important cellular machinery and discuss the relevant clinical implications.http://journal.frontiersin.org/article/10.3389/fmolb.2017.00039/fullAAA ATPasep97/VCPCdc48chaperonesprotein denaturationprotein quality control |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yihong Ye Wai Kwan Tang Ting Zhang Di Xia |
spellingShingle |
Yihong Ye Wai Kwan Tang Ting Zhang Di Xia A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase Frontiers in Molecular Biosciences AAA ATPase p97/VCP Cdc48 chaperones protein denaturation protein quality control |
author_facet |
Yihong Ye Wai Kwan Tang Ting Zhang Di Xia |
author_sort |
Yihong Ye |
title |
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase |
title_short |
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase |
title_full |
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase |
title_fullStr |
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase |
title_full_unstemmed |
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase |
title_sort |
mighty “protein extractor” of the cell: structure and function of the p97/cdc48 atpase |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Molecular Biosciences |
issn |
2296-889X |
publishDate |
2017-06-01 |
description |
p97/VCP (known as Cdc48 in S. cerevisiae or TER94 in Drosophila) is one of the most abundant cytosolic ATPases. It is highly conserved from archaebacteria to eukaryotes. In conjunction with a large number of cofactors and adaptors, it couples ATP hydrolysis to segregation of polypeptides from immobile cellular structures such as protein assemblies, membranes, ribosome, and chromatin. This often results in proteasomal degradation of extracted polypeptides. Given the diversity of p97 substrates, this “segregase” activity has profound influence on cellular physiology ranging from protein homeostasis to DNA lesion sensing, and mutations in p97 have been linked to several human diseases. Here we summarize our current understanding of the structure and function of this important cellular machinery and discuss the relevant clinical implications. |
topic |
AAA ATPase p97/VCP Cdc48 chaperones protein denaturation protein quality control |
url |
http://journal.frontiersin.org/article/10.3389/fmolb.2017.00039/full |
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