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The cell adhesion molecule L1 interacts with nuclear proteins via its intracellular domain

Maria Girbes Minguez1, Gerrit Wolters-Eisfeld1, David Lutz1

  • 1Zentrum für Molekulare Neurobiologie, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|June 14, 2020
PubMed

Insights

A fragment of the cell adhesion molecule L1 (L1) enters the nucleus and binds to proteins involved in gene regulation and DNA repair. These interactions suggest L1 fragments play roles in nervous system nuclear functions.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • The cell adhesion molecule L1 (L1) undergoes proteolytic cleavage in the brain.
  • A 30 kDa fragment of L1, containing its intracellular domain, is imported into the nucleus.

Purpose of the Study:

  • To identify nuclear proteins that interact with the intracellular L1 domain.
  • To investigate the functional implications of L1 nuclear import in the nervous system.

Main Methods:

  • Affinity chromatography using recombinant L1 intracellular domain and mouse brain nuclear extract.
  • Co-immunoprecipitation and enzyme-linked immunosorbent assay (ELISA) with recombinant proteins.
  • Proximity ligation assay in cultured cerebellar granule cells.

Main Results:

  • Identified nuclear L1 binding partners involved in transcriptional regulation, RNA processing, DNA repair, chromatin remodeling, and nucleocytoplasmic transport.
  • Verified direct interactions between L1 and non-POU domain containing octamer-binding protein (NONO) and splicing factor proline/glutamine-rich (SFPQ).
  • Confirmed close interaction between L1 and these partners in cerebellar neurons.

Conclusions:

  • L1 fragments are involved in regulating multiple nuclear functions within the nervous system.
  • These interactions may play roles in chromatin structure, gene expression, RNA processing, and DNA repair.
  • Potential physiological and pathological significance of nuclear L1 fragments in neurological processes.

Keywords:
DNA/RNA-binding proteinsDrosophila behavior/human splicing (DBHS) proteinscell adhesion molecule L1nuclear importproteolytic processing

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