Exocyst-mediated membrane trafficking of the lissencephaly-associated ECM receptor dystroglycan is required for proper brain compartmentalization

Abstract
Data availability
Article and author information
Metrics

Abstract

To assemble a brain, differentiating neurons must make proper connections and establish specialized brain compartments. Abnormal levels of cell adhesion molecules disrupt these processes. Dystroglycan (Dg) is a major non-integrin cell adhesion receptor, deregulation of which is associated with dramatic neuroanatomical defects such as lissencephaly type II, or cobblestone brain. The previously established Drosophila model for cobblestone encephaly was used to understand how Dg is regulated in the brain. During development, Dg has a spatiotemporally dynamic expression pattern, fine-tuning of which is crucial for accurate brain assembly. In addition, mass spectrometry analyses identified numerous components associated with Dg in neurons, including several proteins of the exocyst complex. Data show that exocyst-based membrane trafficking of Dg allows its distinct expression pattern, essential for proper brain morphogenesis. Further studies of the Dg neuronal interactome will allow identification of new factors involved in the development of dystroglycanopathies and advance disease diagnostics in humans.

Data availability

The authors declare that all data supporting the findings of this study are available within the article and its supplementary information files or found on the Dryad Digital Repository (Data DOI: doi:10.5061/dryad.8sf7m0cmf).

The following data sets were generated

(2021) Neuronal Dystroglycan Interactome
Dryad Digital Repository, doi:10.5061/dryad.8sf7m0cmf.

http://dx.doi.org/10.5061/dryad.8sf7m0cmf

Article and author information

Author details

Andriy S Yatsenko

Institute of Cell Biochemistry, Hannover Medical School, Hannover, Germany

Competing interests
The authors declare that no competing interests exist.
Mariya M Kucherenko

Institute of Physiology, Charite Medicine University, Berlin, Germany

Competing interests
The authors declare that no competing interests exist.
Yuanbin Xie

Department of Biochemistry and Molecular Biology, School of Basic Medical Science, Gannan Medical University, Ganzhou, China

Competing interests
The authors declare that no competing interests exist.
Henning Urlaub

Bioanalytics, Institute of Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany

Competing interests
The authors declare that no competing interests exist.
Halyna R Shcherbata

Institute of Cell Biochemistry, Hannover Medical School, Hannover, Germany

For correspondence
halyna.shcherbata@mpibpc.mpg.de

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-3855-0345

Funding

EMBO (YIP)

Halyna R Shcherbata

VW Stiftung (AZN3008)

Halyna R Shcherbata

Hannover Medical School

Halyna R Shcherbata

VW Stiftung (AZ97750)

Halyna R Shcherbata

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.