Open Access Open Badges Research

Genome-wide analysis links emerin to neuromuscular junction activity in Caenorhabditis elegans

Cristina González-Aguilera14, Kohta Ikegami2, Cristina Ayuso1, Alberto de Luis3, María Íñiguez3, Juan Cabello3, Jason D Lieb2 and Peter Askjaer1*

Author Affiliations

1 Andalusian Center for Developmental Biology (CABD), CSIC/JA/Universidad Pablo de Olavide, 41013 Seville, Spain

2 Department of Biology and Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, 27599 Chapel Hill, NC, USA

3 Center for Biomedical Research of La Rioja (CIBIR), 26006 Logroño, Spain

4 Current address: Biotech Research and Innovation Centre, University of Copenhagen, 2200 Copenhagen, Denmark

For all author emails, please log on.

Genome Biology 2014, 15:R21  doi:10.1186/gb-2014-15-2-r21

Published: 3 February 2014



Laminopathies are diseases characterized by defects in nuclear envelope structure. A well-known example is Emery-Dreifuss muscular dystrophy, which is caused by mutations in the human lamin A/C and emerin genes. While most nuclear envelope proteins are ubiquitously expressed, laminopathies often affect only a subset of tissues. The molecular mechanisms underlying these tissue-specific manifestations remain elusive. We hypothesize that different functional subclasses of genes might be differentially affected by defects in specific nuclear envelope components.


Here we determine genome-wide DNA association profiles of two nuclear envelope components, lamin/LMN-1 and emerin/EMR-1 in adult Caenorhabditis elegans. Although both proteins bind to transcriptionally inactive regions of the genome, EMR-1 is enriched at genes involved in muscle and neuronal function. Deletion of either EMR-1 or LEM-2, another integral envelope protein, causes local changes in nuclear architecture as evidenced by altered association between DNA and LMN-1. Transcriptome analyses reveal that EMR-1 and LEM-2 are associated with gene repression, particularly of genes implicated in muscle and nervous system function. We demonstrate that emr-1, but not lem-2, mutants are sensitive to the cholinesterase inhibitor aldicarb, indicating altered activity at neuromuscular junctions.


We identify a class of elements that bind EMR-1 but do not associate with LMN-1, and these are enriched for muscle and neuronal genes. Our data support a redundant function of EMR-1 and LEM-2 in chromatin anchoring to the nuclear envelope and gene repression. We demonstrate a specific role of EMR-1 in neuromuscular junction activity that may contribute to Emery-Dreifuss muscular dystrophy in humans.