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Cell environment shapes TDP-43 function with implications in neuronal and muscle disease

  • NYGC ALS Consortium
  • International Centre for Genetic Engineering and Biotechnology
  • Generatio GmbH
  • University College London
  • New York Genome Cente
  • Temple University
  • University of California at Los Angeles
  • Pennsylvania State University
  • Henry Ford Health System
  • University of Pennsylvania
  • Columbia University
  • Massachusetts Institute of Technology
  • Johns Hopkins University
  • Academic Medical Center
  • Leiden University
  • Massachusetts General Hospital
  • Harvard University
  • Board of Governors Regenerative Medicine Institute
  • Cedars-Sinai Medical Center
  • University of Pennsylvania
  • Academy of Athens
  • National and Kapodistrian University of Athens
  • University of Edinburgh
  • Queen Mary University of London
  • Mid and South Essex NHS Foundation Trust
  • Cold Spring Harbor Laboratory
  • Broad Institute
  • Icahn School of Medicine at Mount Sinai
  • University of California at San Francisco
  • Weizmann Institute of Science
  • Washington University St. Louis
  • University of Thessaly
  • St. Joseph's Hospital and Medical Center, Phoenix
  • Hospital for Special Surgery - New York
  • University of Amsterdam
  • Georgetown University
  • University of California at San Diego
  • University of California at Irvine

Research output: Contribution to journal › Article › peer-review

47 Scopus citations

Abstract

TDP-43 (TAR DNA-binding protein 43) aggregation and redistribution are recognised as a hallmark of amyotrophic lateral sclerosis and frontotemporal dementia. As TDP-43 inclusions have recently been described in the muscle of inclusion body myositis patients, this highlights the need to understand the role of TDP-43 beyond the central nervous system. Using RNA-seq, we directly compare TDP-43-mediated RNA processing in muscle (C2C12) and neuronal (NSC34) mouse cells. TDP-43 displays a cell-type-characteristic behaviour targeting unique transcripts in each cell-type, which is due to characteristic expression of RNA-binding proteins, that influence TDP-43’s performance and define cell-type specific splicing. Among splicing events commonly dysregulated in both cell lines, we identify some that are TDP-43-dependent also in human cells. Inclusion levels of these alternative exons are altered in tissues of patients suffering from FTLD and IBM. We therefore propose that TDP-43 dysfunction contributes to disease development either in a common or a tissue-specific manner.

Original languageEnglish
Article number314
JournalCommunications Biology
Volume5
Issue number1
DOIs
StatePublished - Dec 2022

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