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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Lamina-associated polypeptide 1: protein interactions and tissue-selective functions.

Ji-Yeon Shin1, William T Dauer2, Howard J Worman1

  • 1Department of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA.

Seminars in Cell & Developmental Biology
|February 11, 2014
PubMed
Summary

Mutations in lamina-associated polypeptide 1 (LAP1) can cause tissue-specific diseases. Studies in mice reveal LAP1

Keywords:
DystoniaLaminMuscular dystrophyNuclear envelopeNuclear membrane

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Widely expressed nuclear envelope proteins can cause tissue-specific diseases when mutated.
  • Lamina-associated polypeptide 1 (LAP1) is an inner nuclear membrane protein interacting with lamins, torsinA, and emerin.
  • LAP1 may act as a signaling hub across the inner nuclear membrane.

Purpose of the Study:

  • To investigate the functional links between LAP1 and its interacting proteins, torsinA and emerin.
  • To explore the role of LAP1 in tissue-selective disease pathogenesis.

Main Methods:

  • In vivo studies using genetically modified mice.
  • Analysis of nuclear envelope protein complexes.

Main Results:

  • Functional links between LAP1 and torsinA in neurons were supported.
  • Functional links between LAP1 and emerin in muscle were supported.
  • Evidence suggests LAP1's role in mediating tissue-specific disease mechanisms.

Conclusions:

  • Tissue-selective diseases from nuclear envelope protein mutations may stem from disrupted protein complexes.
  • LAP1 plays a crucial role in the selective disruption of these complexes, contributing to disease phenotypes.