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Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Imaging ATG9A, a Multi-Spanning Membrane Protein
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Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

Ataxin-2 associates with rough endoplasmic reticulum.

Simone van de Loo1, Florian Eich, David Nonis

  • 1Section for Molecular Neurogenetics, Department of Neurology, University Hospital, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany.

Experimental Neurology
|November 1, 2008
PubMed
Summary

Ataxin-2, implicated in Spinocerebellar ataxia type 2 (SCA2), is found in the cytoplasm and associated with the endoplasmic reticulum. This suggests a role in mRNA processing and translation regulation.

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Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
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Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

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Last Updated: Jun 28, 2026

Imaging ATG9A, a Multi-Spanning Membrane Protein
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Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
08:55

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

Published on: October 28, 2016

Area of Science:

  • Molecular biology
  • Neuroscience
  • Cell biology

Background:

  • Ataxin-2 is a protein associated with Spinocerebellar ataxia type 2 (SCA2), a neurodegenerative disease.
  • The protein contains a polyglutamine (polyQ) domain, which can expand and cause disease.

Purpose of the Study:

  • To investigate the cellular functions of ataxin-2.
  • To determine the subcellular localization and potential roles of ataxin-2 in neuronal and non-neuronal cells.

Main Methods:

  • Immunocytochemistry and fluorescence microscopy in various cell types.
  • Confocal microscopy for co-localization studies.
  • Subcellular fractionation of mouse brain homogenates.

Main Results:

  • Endogenous and transfected ataxin-2 show cytoplasmic distribution with perinuclear preference and granular appearance.
  • Ataxin-2 co-localizes with endoplasmic reticulum (ER) markers.
  • Pathogenic ataxin-2 with expanded polyQ domain exhibits similar localization.
  • Ataxin-2 associates with rough ER (rER) membranes, dependent on RNA, salt, and phosphorylation.
  • Findings align with ataxin-2 interaction with poly(A)-binding protein (PABP) and its association with polyribosomes and stress granules.

Conclusions:

  • Ataxin-2 is localized to the endoplasmic reticulum and associated with mRNA-binding proteins.
  • These findings suggest ataxin-2 plays a role in mRNA processing and/or translation regulation.
  • Understanding ataxin-2 function may provide insights into SCA2 pathogenesis.