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Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
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Complementary chimeric isoforms reveal Dscam1 binding specificity in vivo.

Wei Wu1, Goran Ahlsen, David Baker

  • 1Department of Biological Chemistry, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095-1662, USA.

Neuron
|May 1, 2012
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Summary
This summary is machine-generated.

Down syndrome cell adhesion molecule 1 (Dscam1) isoforms mediate self-avoidance in neurons. Altering Dscam1 binding specificity disrupts this crucial process for neural circuit assembly, confirming recognition

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Down syndrome cell adhesion molecule 1 (Dscam1) generates numerous isoforms via alternative splicing.
  • Dscam1 isoforms exhibit isoform-specific homophilic binding in vitro.
  • The role of Dscam1 recognition specificity in vivo for neural circuit assembly remains unclear.

Purpose of the Study:

  • To investigate the in vivo function of Dscam1 isoform recognition specificity.
  • To determine if altered Dscam1 binding properties affect self-avoidance.

Main Methods:

  • Generated chimeric Dscam1 isoforms with altered binding specificities (heterophilic binding).
  • Assessed the ability of these altered isoforms to support neuronal self-avoidance in vivo.
  • Coexpressed complementary Dscam1 isoforms to restore homophilic binding.

Main Results:

  • Chimeric Dscam1 isoforms with heterophilic binding failed to support or poorly supported self-avoidance.
  • Coexpression of complementary Dscam1 isoforms restored self-avoidance.
  • Demonstrated that Dscam1 isoform recognition is essential for self-avoidance.

Conclusions:

  • Isoform-specific recognition between Dscam1 molecules on neuronal processes is critical for self-avoidance.
  • This molecular recognition mechanism underlies proper neural circuit formation.