Ring of change: CDC48/p97 drives protein dynamics at chromatin
The dynamic composition of proteins associated with nuclear DNA is a fundamental property of chromosome biology. In the chromatin compartment dedicated protein complexes govern the accurate synthesis and repair of the genomic information and define the state of DNA compaction in vital cellular proce...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2016-05-01
|
| Series: | Frontiers in Genetics |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fgene.2016.00073/full |
| _version_ | 1811220435210076160 |
|---|---|
| author | André eFranz Leena eAckermann Thorsten eHoppe |
| author_facet | André eFranz Leena eAckermann Thorsten eHoppe |
| author_sort | André eFranz |
| collection | DOAJ |
| description | The dynamic composition of proteins associated with nuclear DNA is a fundamental property of chromosome biology. In the chromatin compartment dedicated protein complexes govern the accurate synthesis and repair of the genomic information and define the state of DNA compaction in vital cellular processes such as chromosome segregation or transcription. Unscheduled or faulty association of proteins with DNA has detrimental consequences on genome integrity. Consequently, the organization of chromatin-bound protein complexes is remarkably dynamic and can respond rapidly to cellular signaling events, which requires tight spatiotemporal control. In this context, the ring-like AAA+ ATPase CDC48/p97 emerges as a key regulator of protein complexes that are marked with ubiquitin or SUMO. Mechanistically, CDC48/p97 functions as a segregase facilitating the extraction of substrate proteins from the chromatin. As such, CDC48/p97 drives molecular reactions either by directed disassembly or rearrangement of chromatin-bound protein complexes. The importance of this mechanism is reflected by human pathologies linked to p97 mutations, including neurodegenerative disorders, oncogenesis, and premature aging. This review focuses on the recent insights into molecular mechanisms that determine CDC48/p97 function in the chromatin environment, which is particularly relevant for cancer and aging research. |
| first_indexed | 2024-04-12T07:42:50Z |
| format | Article |
| id | doaj.art-fdb4985d44ff4c6f857e0cea4129c2a0 |
| institution | Directory Open Access Journal |
| issn | 1664-8021 |
| language | English |
| last_indexed | 2024-04-12T07:42:50Z |
| publishDate | 2016-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Genetics |
| spelling | doaj.art-fdb4985d44ff4c6f857e0cea4129c2a02022-12-22T03:41:47ZengFrontiers Media S.A.Frontiers in Genetics1664-80212016-05-01710.3389/fgene.2016.00073194837Ring of change: CDC48/p97 drives protein dynamics at chromatinAndré eFranz0Leena eAckermann1Thorsten eHoppe2Institute for Genetics and CECAD Cluster of Excellence, University of CologneInstitute for Genetics and CECAD Cluster of Excellence, University of CologneInstitute for Genetics and CECAD Cluster of Excellence, University of CologneThe dynamic composition of proteins associated with nuclear DNA is a fundamental property of chromosome biology. In the chromatin compartment dedicated protein complexes govern the accurate synthesis and repair of the genomic information and define the state of DNA compaction in vital cellular processes such as chromosome segregation or transcription. Unscheduled or faulty association of proteins with DNA has detrimental consequences on genome integrity. Consequently, the organization of chromatin-bound protein complexes is remarkably dynamic and can respond rapidly to cellular signaling events, which requires tight spatiotemporal control. In this context, the ring-like AAA+ ATPase CDC48/p97 emerges as a key regulator of protein complexes that are marked with ubiquitin or SUMO. Mechanistically, CDC48/p97 functions as a segregase facilitating the extraction of substrate proteins from the chromatin. As such, CDC48/p97 drives molecular reactions either by directed disassembly or rearrangement of chromatin-bound protein complexes. The importance of this mechanism is reflected by human pathologies linked to p97 mutations, including neurodegenerative disorders, oncogenesis, and premature aging. This review focuses on the recent insights into molecular mechanisms that determine CDC48/p97 function in the chromatin environment, which is particularly relevant for cancer and aging research.http://journal.frontiersin.org/Journal/10.3389/fgene.2016.00073/fullChromatinDNA RepairUbiquitinreplicationSUMOCdc48 |
| spellingShingle | André eFranz Leena eAckermann Thorsten eHoppe Ring of change: CDC48/p97 drives protein dynamics at chromatin Frontiers in Genetics Chromatin DNA Repair Ubiquitin replication SUMO Cdc48 |
| title | Ring of change: CDC48/p97 drives protein dynamics at chromatin |
| title_full | Ring of change: CDC48/p97 drives protein dynamics at chromatin |
| title_fullStr | Ring of change: CDC48/p97 drives protein dynamics at chromatin |
| title_full_unstemmed | Ring of change: CDC48/p97 drives protein dynamics at chromatin |
| title_short | Ring of change: CDC48/p97 drives protein dynamics at chromatin |
| title_sort | ring of change cdc48 p97 drives protein dynamics at chromatin |
| topic | Chromatin DNA Repair Ubiquitin replication SUMO Cdc48 |
| url | http://journal.frontiersin.org/Journal/10.3389/fgene.2016.00073/full |
| work_keys_str_mv | AT andreefranz ringofchangecdc48p97drivesproteindynamicsatchromatin AT leenaeackermann ringofchangecdc48p97drivesproteindynamicsatchromatin AT thorstenehoppe ringofchangecdc48p97drivesproteindynamicsatchromatin |