Keyword search (3,254 papers available)


Multi-tissue patterning drives anterior morphogenesis of the C. elegans embryo.

Author(s): Grimbert S, Mastronardi K, Richard V, Christensen R, Law C, Zardoui K, Fay D, Piekny A

Complex structures derived from multiple tissue types are challenging to study in vivo, and our knowledge of how cells from different tissues are coordinated is limited. Model organisms have proven invaluable for improving our understanding of how chemical ...

Article GUID: 33309948

The phenotype associated with variants in TANGO2 may be explained by a dual role of the protein in ER-to-Golgi transport and at the mitochondria.

Author(s): Milev MP, Saint-Dic D, Zardoui K, Klopstock T, Law C, Distelmaier F, Sacher M

TANGO2 variants result in a complex disease phenotype consisting of recurrent crisis-induced rhabdomyolysis, encephalopathy, seizures, lactic acidosis, hypoglycemia, and cardiac arrhythmias. Although first described in a fruit fly model as a protein necessa...

Article GUID: 32909282

Photosystem Biogenesis Is Localized to the Translation Zone in the Chloroplast of Chlamydomonas.

Author(s): Sun Y, Valente-Paterno MI, Bakhtiari S, Law C, Zhan Y, Zerges W

Photosystem Biogenesis Is Localized to the Translation Zone in the Chloroplast of Chlamydomonas.

Plant Cell. 2019 Oct 07;:

Authors: Sun Y, Valente-Paterno MI, Bakhtiari S, Law C, Zhan Y, Zerges W

Abstract
Intracellular pro...

Article GUID: 31591163

Active Ran regulates anillin function during cytokinesis.

Author(s): Beaudet D, Akhshi T, Phillipp J, Law C, Piekny A

Mol Biol Cell. 2017 Nov 15;28(24):3517-3531 Authors: Beaudet D, Akhshi T, Phillipp J, Law C, Piekny A

Article GUID: 28931593


Title:The phenotype associated with variants in TANGO2 may be explained by a dual role of the protein in ER-to-Golgi transport and at the mitochondria.
Authors:Milev MPSaint-Dic DZardoui KKlopstock TLaw CDistelmaier FSacher M
Link:https://www.ncbi.nlm.nih.gov/pubmed/32909282
Category:J Inherit Metab Dis
PMID:32909282
Dept Affiliation: BIOLOGY
1 Department of Biology, Concordia University, Montreal Quebec, Canada.
2 Department of Neurology, Friedrich-Baur-Institute, Ludwig-Maximilians-University, Munich, Germany.
3 German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
4 Munich Cluster for Systems Neurology (SyNergy), Munich, Germany.
5 Centre for Microscopy and Cellular Imaging, Concordia University, Quebec, Canada.
6 Department of General Pediatrics, Neonatology and Pediatric Cardiology, University Children's Hospital Düsseldorf, Medical faculty, Heinrich Heine University, Düsseldorf, Germany.
7 Department of Anatomy and Cell Biology, McGill University, Quebec, Canada.

Description:

The phenotype associated with variants in TANGO2 may be explained by a dual role of the protein in ER-to-Golgi transport and at the mitochondria.

J Inherit Metab Dis. 2020 Sep 10; :

Authors: Milev MP, Saint-Dic D, Zardoui K, Klopstock T, Law C, Distelmaier F, Sacher M

Abstract

TANGO2 variants result in a complex disease phenotype consisting of recurrent crisis-induced rhabdomyolysis, encephalopathy, seizures, lactic acidosis, hypoglycemia, and cardiac arrhythmias. Although first described in a fruit fly model as a protein necessary for some aspect of Golgi function and organization, its role in the cell at a fundamental level has not been addressed. Such studies are necessary to better counsel families regarding treatment options and nutrition management to mitigate the metabolic aspects of the disease. The few studies performed to address the pathway(s) in which TANGO2 functions have led to enigmatic results, with some suggesting defects in membrane traffic while others suggest unknown mitochondrial defects. Here, we have performed a robust membrane trafficking assay on fibroblasts derived from three different individuals harboring TANGO2 variants and show that there is a significant delay in the movement of cargo between the endoplasmic reticulum and the Golgi. Importantly, this delay was attributed to a defect in TANGO2 function. We further show that a portion of TANGO2 protein localizes to the mitochondria through a necessary but not sufficient stretch of amino acids at the amino terminus of the protein. Fibroblasts from affected individuals also displayed changes in mitochondrial morphology. We conclude that TANGO2 functions in both membrane trafficking and in some as yet undetermined role in mitochondria physiology. The phenotype of affected individuals can be partially explained by this dual involvement of the protein. This article is protected by copyright. All rights reserved.

PMID: 32909282 [PubMed - as supplied by publisher]