Interaction between emerin and nuclear lamins.

Abstract

Emerin is an inner nuclear membrane protein that is involved in X-linked recessive Emery-Dreifuss muscular dystrophy (X-EDMD). Although the function of this protein is still unknown, we revealed that C-terminus transmembrane domain-truncated emerin (amino acid 1-225) binds to lamin A with higher affinity than lamin C. Screening for the emerin binding protein and immunoprecipitation analysis showed that lamin A binds to emerin specifically. We also used the yeast two-hybrid system to clarify that this interaction requires the top half of the tail domain (amino acid 384-566) of lamin A. Lamin A and lamin C are alternative splicing products of the lamin A/C gene that is responsible for autosomal dominant Emery-Dreifuss muscular dystrophy (AD-EDMD). These results indicate that the emerin-lamin interaction requires the tail domains of lamin A and lamin C. The data also suggest that the lamin A-specific region (amino acids 567-664) plays some indirect role in the difference in emerin-binding capacity between lamin A and lamin C. This is the first report that refers the difference between lamin A and lamin C in the interaction with emerin. These data also suggest that lamin A is important for nuclear membrane integrity.

• Authors: M Sakaki, H Koike, N Takahashi, N Sasagawa, S Tomioka, K Arahata, S Ishiura
• Journal: Journal of biochemistry (J Biochem) Vol. 129 Issue 2 Pg. 321-7 (Feb 2001) ISSN: 0021-924X [Print] England
• PMID: 11173535 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Lamin Type A
• Lamins
• Membrane Proteins
• Nuclear Proteins
• Thymopoietins
• emerin
• lamin C

Topics

• Animals
• In Vitro Techniques
• Lamin Type A
• Lamins
• Liver (cytology, metabolism)
• Membrane Proteins (chemistry, genetics, metabolism)
• Muscles (cytology, metabolism)
• Nuclear Envelope (chemistry, physiology)
• Nuclear Proteins (chemistry, genetics, metabolism)
• Protein Binding (physiology)
• Rats
• Sequence Analysis, Protein
• Thymopoietins (chemistry, genetics, metabolism)
• Two-Hybrid System Techniques (statistics & numerical data)