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The protein encoded by vcp is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. Additionally we are shipping Valosin Containing Protein Antibodies (150) and Valosin Containing Protein Kits (19) and many more products for this protein.
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The findings of the present study indicated that VCP is very important for the proliferation and metastasis of colorectal cancer; therefore, targeting VCP and its downstream targets may represent novel therapies for the treatment of colorectal cancer.
Timely and efficient degradation of ubiquitinated IkappaB[alpha], concomitant with timely and efficient liberation of RelA (show NFkBP65 Proteins) from ubiquitinated IkappaB[alpha] and RelA (show NFkBP65 Proteins) nuclear translocation, essentially depends on the presence of functional p97/VCP.
results have revealed SUMOylation as a molecular signaling switch to regulate the distribution and functions of VCP during stress response, and suggest that deficiency in VCP SUMOylation caused by pathogenic mutations will render cells vulnerable to stress insults.
depletion of VCP enzymatic activity triggers cancer cell death in part through inadequate regulation of protein synthesis and amino acid metabolism.
new role of VCP/p97 segregase in the timely processing of ubiquitinated CSB (show ERCC6 Proteins) from damaged chromatin.
Ankrd13 proteins cooperate with VCP to regulate the lysosomal trafficking of ubiquitinated Cav-1 (show CAV1 Proteins).
results suggest that human Cdc48 interacts functionally with the 20S proteasome (show PSMA5 Proteins).
we show that loss of VCP induces endoplasmic reticulum stress and epithelial-mesenchymal transition
interaction between SelK (show HSP Proteins) and p97(VCP) is SelS (show SELS Proteins)-dependent, and the resulting ERAD complex (SelS (show SELS Proteins)-p97(VCP)-SelK (show HSP Proteins)) plays an important role in ERAD and ER stress
this study demonstrates significant correlation between the cytoplasmic expression of VCP and adverse prognosis in breast carcinoma, suggesting that VCP may serve as a prognostic biomarker in breast carcinoma.
results suggest that (i) NLRP3 inflammasome and local IL-1beta((+))F4/80((+))Ly6C((+)) inflammatory macrophages contribute to pathogenesis of VCP-associated myopathy
VCP (valosin-containing protein), together with its cofactor P47 (show MFGE8 Proteins) and the endoplasmic reticulum (ER) morphology regulator ATL1 (Atlastin-1 (show ATL1 Proteins)), regulates tubular ER formation
Lysine Methylation of the Valosin-Containing Protein (VCP) Is Dispensable for Development and Survival of Mice
Global expression profiling of VCP(R155H/+) mice identified key dysregulated signaling pathways including genes involved in the physiological system development and function, diseases and disorders, and molecular and cellular functions.
The results reveal an unexpected, crucial role of ATP consumption by VCP in determining cell fate in retinitis pigmentosa, and point to a promising new neuroprotective strategy for this currently incurable disease.
Pro(178) and Pro(183) of SelS (show SELS Proteins) play important roles in the translocation of p97(VCP) to the ER membrane and protect cells from ER stress
Knockdown or chemical inhibition of p97 (show EIF4G2 Proteins) causes robust accumulation of USP33 (show USP33 Proteins) due to inhibition of its degradation
conclude that the Akt (show AKT1 Proteins) substrate, VCP, mediates the increased expression of iNOS (show NOS2 Proteins) downstream from Hsp22 (show HSPB8 Proteins) through an NF-kappaB (show NFKB1 Proteins)-dependent mechanism
Molecular dynamics simulations are used to probe energetic requirements of substrate protein translocation through the p97 (show EIF4G2 Proteins) pore and mechanisms of substrate binding and release from p97 (show EIF4G2 Proteins) subunits during the allosteric cycle.
Data indicate that genetic ablation or chemical inhibition of p97 does not diminish DRiP antigen presentation nor does it alter the levels of MHC class I molecules on the cell surface.
p97 is an essential regulator of DNA damage-dependent CDT1 (show CDT1 Proteins) destruction
CDC-48/p97 coordinates CDT-1 (show CDT1 Proteins) degradation with GINS chromatin dissociation to ensure faithful DNA replication
data reveal an essential pathway that regulates reformation of the nucleus after mitosis and defines ubiquitin-dependent protein extraction as a common mechanism of Cdc48/p97 activity also during nucleus formation
results suggest that VCP plays a mechanistic role in releasing WRNp from the nucleolus
When we introduced CDC48 antisense morpholino oligonucleotides into zebrafish embryos, the morphant embryos were lethal and showed defects in neuronal outgrowth and neurodegeneration.
CDC48 may promote cell cycling and cell proliferation via C-terminal tyrosine phosphorylation during cold acclimation in fish cells
The protein encoded by this gene is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. This protein, as a structural protein, is associated with clathrin, and heat-shock protein Hsc70, to form a complex. It has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation.
transitional endoplasmic reticulum ATPase
, valosin-containing protein
, valosin containing protein
, 15S Mg(2+)-ATPase p97 subunit
, TER ATPase
, yeast Cdc48p homolog
, AAA ATPase p97
, Inv protein
, homolog of yeast cdc48
, p97 ATPase