TY - JOUR
T1 - Np9 protein of human endogenous retrovirus K interacts with ligand of numb protein X
AU - Armbruester, Vivienne
AU - Sauter, Marlies
AU - Roemer, Klaus
AU - Best, Barbara
AU - Hahn, Steffen
AU - Nty, Achille
AU - Schmid, Andreas
AU - Philipp, Stephan
AU - Mueller, Anja
AU - Mueller-Lantzsch, Nikolaus
PY - 2004
Y1 - 2004
N2 - We have recently identified Np9 as a novel nuclear protein produced by the human endogenous retrovirus K and were able to document the exclusive presence of np9 transcript in tumors and transformed cells. With the aim of studying whether Np9 has a role in tumorigenesis, a systematic search for interacting proteins was performed. Here, we identify the RING-type E3 ubiquitin ligase LNX (ligand of Numb protein X) as an Np9-interacting partner. We furthermore show that the interaction involves N- and C-terminal domains of both proteins and can affect the subcellular localization of LNX. LNX has been reported to target the cell fate determinant and Notch antagonist Numb for proteasome-dependent degradation, thereby causing an increase in transactivational activity of Notch. We document that LNX-interacting Np9, like Numb, is unstable and degraded via the proteasome pathway and that ectopic Numb can stabilize recombinant Np9. Combined, these findings point to the possibility that Np9 affects tumorigenesis through the LNX/Numb/Notch pathway.
AB - We have recently identified Np9 as a novel nuclear protein produced by the human endogenous retrovirus K and were able to document the exclusive presence of np9 transcript in tumors and transformed cells. With the aim of studying whether Np9 has a role in tumorigenesis, a systematic search for interacting proteins was performed. Here, we identify the RING-type E3 ubiquitin ligase LNX (ligand of Numb protein X) as an Np9-interacting partner. We furthermore show that the interaction involves N- and C-terminal domains of both proteins and can affect the subcellular localization of LNX. LNX has been reported to target the cell fate determinant and Notch antagonist Numb for proteasome-dependent degradation, thereby causing an increase in transactivational activity of Notch. We document that LNX-interacting Np9, like Numb, is unstable and degraded via the proteasome pathway and that ectopic Numb can stabilize recombinant Np9. Combined, these findings point to the possibility that Np9 affects tumorigenesis through the LNX/Numb/Notch pathway.
U2 - 10.1128/JVI.78.19.10310-10319.2004
DO - 10.1128/JVI.78.19.10310-10319.2004
M3 - Article
VL - 78
SP - 10310
EP - 10319
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 19
ER -