NVL2 Is a Nucleolar AAA-ATPase that Interacts with Ribosomal Protein L5 through Its Nucleolar Localization Sequence
AUTOR(ES)
Nagahama, Masami
FONTE
The American Society for Cell Biology
RESUMO
NVL (nuclear VCP-like protein), a member of the AAA-ATPase family, is known to exist in two forms with N-terminal extensions of different lengths in mammalian cells. Here, we show that they are localized differently in the nucleus; NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Mutational analysis demonstrated the presence of two nuclear localization signals in NVL2, one of which is shared with NVL1. In addition, a nucleolar localization signal was found to exist in the N-terminal extra region of NVL2. The nucleolar localization signal is critical for interaction with ribosomal protein L5, which was identified as a specific interaction partner of NVL2 on yeast two-hybrid screening. The interaction of NVL2 with L5 is ATP-dependent and likely contributes to the nucleolar translocation of NVL2. The physiological implication of this interaction was suggested by the finding that a dominant negative NVL2 mutant inhibits ribosome biosynthesis, which is known to take place in the nucleolus.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=532049Documentos Relacionados
- AAA-ATPase p97/Cdc48p, a Cytosolic Chaperone Required for Endoplasmic Reticulum-Associated Protein Degradation
- The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes.
- Interaction of the HIV-1 Rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5
- U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and mammals.
- DNA Damage Modulates Nucleolar Interaction of the Werner Protein with the AAA ATPase p97/VCP