Structural Insights Into TDP-43 and Effects of Post-translational Modifications

Liberty François-Moutal, Samantha Perez-Miller, David D. Scott, Victor G. Miranda, Niloufar Mollasalehi, May Khanna

Research output: Contribution to journalReview article

2 Scopus citations

Abstract

Transactive response DNA binding protein (TDP-43) is a key player in neurodegenerative diseases. In this review, we have gathered and presented structural information on the different regions of TDP-43 with high resolution structures available. A thorough understanding of TDP-43 structure, effect of modifications, aggregation and sites of localization is necessary as we develop therapeutic strategies targeting TDP-43 for neurodegenerative diseases. We discuss how different domains as well as post-translational modification may influence TDP-43 overall structure, aggregation and droplet formation. The primary aim of the review is to utilize structural insights as we develop an understanding of the deleterious behavior of TDP-43 and highlight locations of established and proposed post-translation modifications. TDP-43 structure and effect on localization is paralleled by many RNA-binding proteins and this review serves as an example of how structure may be modulated by numerous compounding elements.

Original languageEnglish (US)
Article number301
JournalFrontiers in Molecular Neuroscience
Volume12
DOIs
StatePublished - Dec 17 2019

Keywords

  • post-translational modification
  • RRM domain
  • structure
  • subdomains
  • TDP-43 = TAR DNA–binding protein 43

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Structural Insights Into TDP-43 and Effects of Post-translational Modifications'. Together they form a unique fingerprint.

  • Cite this