| NPLOC4 is a potential target and a poor prognostic signature in lung squamous cell carcinoma. | NPLOC4 is a potential target and a poor prognostic signature in lung squamous cell carcinoma.
Wang N, Zhu D, Liu Y, Wu J, Wang M, Jin S, Fu F, Li B, Ji H, Du C, Zheng Z., Free PMC Article | 11/27/2023 |
| Structural basis for the interaction between human Npl4 and Npl4-binding motif of human Ufd1. | Structural basis for the interaction between human Npl4 and Npl4-binding motif of human Ufd1.
Nguyen TQ, My Le LT, Kim DH, Ko KS, Lee HT, Kim Nguyen YT, Kim HS, Han BW, Kang W, Yang JK. | 11/12/2022 |
| Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase. | Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase.
Fujisawa R, Polo Rivera C, Labib KPM., Free PMC Article | 08/20/2022 |
| Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative. | Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative.
Pan M, Zheng Q, Yu Y, Ai H, Xie Y, Zeng X, Wang C, Liu L, Zhao M., Free PMC Article | 01/16/2021 |
| Targeting NPL4 via drug repositioning using disulfiram for the treatment of clear cell renal cell carcinoma. | Targeting NPL4 via drug repositioning using disulfiram for the treatment of clear cell renal cell carcinoma.
Yoshino H, Yamada Y, Enokida H, Osako Y, Tsuruda M, Kuroshima K, Sakaguchi T, Sugita S, Tatarano S, Nakagawa M., Free PMC Article | 09/19/2020 |
| Multisystem proteinopathy mutations in VCP/p97 increase NPLOC4-UFD1L binding and substrate processing. | Multisystem Proteinopathy Mutations in VCP/p97 Increase NPLOC4·UFD1L Binding and Substrate Processing.
Blythe EE, Gates SN, Deshaies RJ, Martin A., Free PMC Article | 07/4/2020 |
| We demonstrate that WT p97 can unfold proteins and that this activity is dependent on the p97 adaptor NPLOC4-UFD1L, ATP hydrolysis, and substrate ubiquitination, with branched chains providing maximal stimulation. | Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy.
Blythe EE, Olson KC, Chau V, Deshaies RJ., Free PMC Article | 05/12/2018 |
| The study revealed a regulatory role of the p97-Npl4-Ufd1 complex in regulating a partial degradation of the NF-kappaB subunit p100. | The Transitional Endoplasmic Reticulum ATPase p97 Regulates the Alternative Nuclear Factor NF-κB Signaling via Partial Degradation of the NF-κB Subunit p100.
Zhang Z, Wang Y, Li C, Shi Z, Hao Q, Wang W, Song X, Zhao Y, Jiao S, Zhou Z., Free PMC Article | 11/7/2015 |
| p97-Ufd1-Npl4 is an integral part of G2/M checkpoint signaling and thereby suppresses chromosome instability. | The p97-Ufd1-Npl4 ATPase complex ensures robustness of the G2/M checkpoint by facilitating CDC25A degradation.
Riemer A, Dobrynin G, Dressler A, Bremer S, Soni A, Iliakis G, Meyer H., Free PMC Article | 10/25/2014 |
| Data indicate that the p97-UFD1L-NPL4 protein complex specifically associates with ubiquitinated IkappaBalpha via the interactions between p97 and the SCF(beta-TRCP) ubiquitin ligase. | The p97-UFD1L-NPL4 protein complex mediates cytokine-induced IκBα proteolysis.
Li JM, Wu H, Zhang W, Blackburn MR, Jin J., Free PMC Article | 03/22/2014 |
| In coordination with the P97-UFD1-NPL4 complex (P97(UFD1/NPL4)), NUB1L promotes transfer of NEDD8 to proteasome for degradation. | NEDD8 ultimate buster-1 long (NUB1L) protein promotes transfer of NEDD8 to proteasome for degradation through the P97UFD1/NPL4 complex.
Liu S, Yang H, Zhao J, Zhang YH, Song AX, Hu HY., Free PMC Article | 01/4/2014 |
| Data indicate that Npl4-Ufd1 heterodimer is required for VCP-FAF1 interaction. | Complex of Fas-associated factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD).
Lee JJ, Park JK, Jeong J, Jeon H, Yoon JB, Kim EE, Lee KJ., Free PMC Article | 05/4/2013 |
| Data establish Cdc48/p97-Ufd1-Npl4 as a crucial negative regulator of Aurora B early in mitosis of human somatic cells and suggest that the activity of Aurora B on chromosomes needs to be restrained to ensure faithful chromosome segregation. | Cdc48/p97-Ufd1-Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells.
Dobrynin G, Popp O, Romer T, Bremer S, Schmitz MH, Gerlich DW, Meyer H. | 09/24/2011 |
| Data suggest that the human cytomegalovirus dislocation reaction in US2 cells is independent of the p97 cofactor Ufd1-Npl4, and different retrotranslocation mechanisms can employ distinct p97 ATPase complexes to dislocate substrates. | The p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.
Soetandyo N, Ye Y., Free PMC Article | 12/11/2010 |
| This favors the model where the Ufd1-Npl4 dimer forms a regulatory gate at the exit from the retrotranslocone, rather than actively promoting retrotranslocation like the p97VCP ATPase. | Analysis of Npl4 deletion mutants in mammalian cells unravels new Ufd1-interacting motifs and suggests a regulatory role of Npl4 in ERAD.
Lass A, McConnell E, Fleck K, Palamarchuk A, Wójcik C. | 01/21/2010 |
| Ufd1-Npl4 is a negative regulator of retrotranslocation, delaying the retrotranslocation of endoplasmic reticulum-associated degradation substrates independently of its association with VCP | Ufd1-Npl4 is a negative regulator of cholera toxin retrotranslocation.
McConnell E, Lass A, Wójcik C. | 01/21/2010 |