p97/CDC48 is a highly abundant hexameric AAA-ATPase that functions as a molecular chaperone in numerous diverse cellular activities. We have identified an Arabidopsis UBX domain-containing protein, PUX1, which functions to regulate the oligomeric structure of the Arabidopsis homolog of p97/CDC48, AtCDC48, as well as mammalian p97. PUX1 is a soluble protein that co-fractionates with non-hexameric AtCDC48 and physically interacts with AtCDC48 in vivo. Binding of PUX1 to AtCDC48 is mediated through the UBX-containing C-terminal domain. However, disassembly of the chaperone is dependent upon the N-terminal domain of PUX1. These findings provide evidence that the assembly and disassembly of the hexameric p97/CDC48 complex is a dynamic process. This new unexpected level of regulation for p97/CDC48 was demonstrated to be critical in vivo as pux1 loss-of-function mutants display accelerated growth relative to wild-type plants. These results suggest a role for AtCDC48 and PUX1 in regulating plant growth.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1074/jbc.M405498200 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Linear ubiquitination at damaged lysosomes induces local NFKB activation and controls cell survival.
Autophagy
January 2025
Institute for Experimental Pediatric Hematology and Oncology, Goethe University Frankfurt, Frankfurt am Main, Germany.
Lysosomes are the major cellular organelles responsible for nutrient recycling and degradation of cellular material. Maintenance of lysosomal integrity is essential for cellular homeostasis and lysosomal membrane permeabilization (LMP) sensitizes toward cell death. Damaged lysosomes are repaired or degraded via lysophagy, during which glycans, exposed on ruptured lysosomal membranes, are recognized by galectins leading to K48- and K63-linked poly-ubiquitination (poly-Ub) of lysosomal proteins followed by recruitment of the macroautophagic/autophagic machinery and degradation.
View Article and Find Full Text PDFComparative Proteome-Wide Abundance Profiling of Yeast Strains Deleted for Cdc48 Adaptors.
Proteomes
October 2024
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
The yeast ATPase Cdc48 (known as p97/VCP in human cells) plays an important role in the Ubiquitin Proteasome System. VCP is essential for cancer cell proliferation, and its dysregulation has been implicated in several neurodegenerative diseases. Cdc48 functions by extracting ubiquitylated proteins from membranes, protein complexes and chromatin by often facilitating their proteasomal degradation.
View Article and Find Full Text PDFUbiquitin regulatory X (UBX) domain-containing protein 6 is essential for autophagy induction and inflammation control in macrophages.
Cell Mol Immunol
December 2024
Department of Microbiology, Chungnam National University College of Medicine, Daejeon, 35015, Republic of Korea.
Article Synopsis
- UBXN6 is a crucial cofactor for p97, involved in various cellular activities, and its role in the innate immune system is not well understood.
- In sepsis patients, UBXN6 levels increase and are linked to lower inflammatory gene activity while promoting autophagy through Forkhead box O3 expression.
- In experiments with mice, lack of UBXN6 in macrophages led to worse inflammation and metabolic changes, indicating UBXN6's importance in regulating immune responses and maintaining proper cellular function during sepsis.
UBXN3B is crucial for B lymphopoiesis.
EBioMedicine
August 2024
Department of Immunology, School of Medicine, UConn Health, Farmington, CT, 06030, USA. Electronic address:
Background: The ubiquitin regulatory X (UBX) domain-containing proteins (UBXNs) are putative adaptors for ubiquitin ligases and valosin-containing protein; however, their in vivo physiological functions remain poorly characterised. We recently showed that UBXN3B is essential for activating innate immunity to DNA viruses and controlling DNA/RNA virus infection. Herein, we investigate its role in adaptive immunity.
View Article and Find Full Text PDFMaize lipid droplet-associated protein 2 is recruited by a virus to enhance viral multiplication and infection through regulating cellular fatty acid metabolism.
Plant J
September 2024
MARA-Key Laboratory of Surveillance and Management for Plant Quarantine Pests, College of Plant Protection, and State Key Laboratory for Maize Bio-breeding, China Agricultural University, Beijing, 100193, China.
Pathogen infection induces massive reprogramming of host primary metabolism. Lipid and fatty acid (FA) metabolism is generally disrupted by pathogens and co-opted for their proliferation. Lipid droplets (LDs) that play important roles in regulating cellular lipid metabolism are utilized by a variety of pathogens in mammalian cells.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!