Identification of FAM96B as a novel prelamin A binding partner.

Abstract

Prelamin A accumulation causes nuclear abnormalities, impairs nuclear functions, and eventually promotes cellular senescence. However, the underlying mechanism of how prelamin A promotes cellular senescence is still poorly understood. Here we carried out a yeast two-hybrid screen using a human skeletal muscle cDNA library to search for prelamin A binding partners, and identified FAM96B as a prelamin A binding partner. The interaction of FAM96B with prelamin A was confirmed by GST pull-down and co-immunoprecipitation experiments. Furthermore, co-localization experiments by fluorescent confocal microscopy revealed that FAM96B colocalized with prelamin A in HEK-293 cells. Taken together, our data demonstrated the physical interaction between FAM96B and prelamin A, which may provide some clues to the mechanisms of prelamin A in premature aging.

• Authors: Xing-Dong Xiong, Junwen Wang, Huiling Zheng, Xia Jing, Zhenjie Liu, Zhongjun Zhou, Xinguang Liu
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 440 Issue 1 Pg. 20-4 (Oct 11 2013) ISSN: 1090-2104 [Electronic] United States
• PMID: 24041693 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Crown Copyright © 2013. Published by Elsevier Inc. All rights reserved.

Chemical References

• CIAO2B protein, human
• Carrier Proteins
• Lamin Type A
• Metalloproteins
• Nuclear Proteins
• Protein Precursors
• prelamin A

Topics

• Carrier Proteins (analysis, metabolism)
• Cellular Senescence
• HEK293 Cells
• Humans
• Lamin Type A
• Metalloproteins
• Nuclear Proteins (analysis, metabolism)
• Progeria (metabolism)
• Protein Binding
• Protein Interaction Maps
• Protein Precursors (analysis, metabolism)
• Two-Hybrid System Techniques