Disc1 Protein Aggregates
Disc1 Protein Aggregates - Related Videos
14:33
Generation, Purification, and Characterization of Cell-invasive DISC1 Protein Species
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Cited by 13 •
2012
The generation, purification and cell invasion of intracellular, cytoplasmic full length DISC1 protein aggresomes from cell cultures and of a labeled, multimeric recombinant DISC1 protein fragment in E. coli are described. Cell invasiveness is shown for recipient cells in cell culture and for neurons in vivo after stereotactical brain inoculation.
11:57
Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
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Cited by 7 •
2017
The goal of the method presented here is to explore protein aggregation during normal aging in the model organism C. elegans. The protocol represents a powerful tool to study the highly insoluble large aggregates that form with age and to determine how changes in proteostasis impact protein aggregation.
09:22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Cited by 21 •
2015
Unmodified and hyperphosphorylated tau proteins were used in two in vitro aggregation assays to reveal the hyperphosphorylation-dependent fast aggregation kinetics. These assays pave the way for future screens for compounds that can modulate the propensity of hyperphosphorylated tau to form fibrils that underlie the progression of Alzheimer’s disease.
04:12
Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor
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2025
In this video, we demonstrate a cell-based protein aggregation assay using proteasome inhibitors, which block proteasome activity, preventing misfolded, mutant proteins, fused to a fluorescent label, from undergoing ubiquitin-dependent proteasomal degradation, leading to their accumulation within the cell cytoplasm. The protein aggregates are then visualized and quantified by fluorescence microscopy.
08:59
4D Imaging of Protein Aggregation in Live Cells
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Cited by 4 •
2013
Cellular viability depends on timely and efficient management of protein misfolding. Here we describe a method for visualizing the different potential fates of a misfolded protein: refolding, degradation, or sequestration in inclusions. We demonstrate the use of a folding sensor, Ubc9ts, for monitoring proteostasis and aggregation quality control in live cells using 4D microscopy.
FAQs
Self-association can progress from individual DISC1 molecules to oligomers and then to larger assemblies. This structural shift may alter the protein’s solubility, where it is distributed within a cell, and which partner proteins it can contact. Because DISC1 acts as a scaffold, these changes provide a mechanistic link between aggregation and altered neuronal signaling or development.
Oligomers are assemblies formed by multiple DISC1 molecules, while larger structures represent a further level of self-associated organization. The distinction matters because increasing assembly can produce progressively different cellular behavior, including changes in solubility, localization, and binding interactions. Comparing these forms helps researchers determine whether DISC1 behavior changes gradually or with a particular assembly state.
DISC1 supports cellular organization through interactions with partner proteins, so aggregation may influence more than DISC1 distribution alone. Altered assembly can change which binding interactions remain available or how they occur. Studying these relationships helps connect a physical change in DISC1 to downstream questions about neuronal signaling, development, and mechanisms relevant to neuropsychiatric disease.
Solubility and cellular distribution indicate how accessible DISC1 may be within the cell and where its scaffold functions could occur. Aggregation-associated changes in either property can therefore suggest altered availability for signaling or developmental roles. Measuring both provides complementary evidence: solubility describes the protein’s physical state, whereas distribution shows its cellular placement.
Studies can assess three connected features: the extent of aggregation, the cellular localization of DISC1, and its binding interactions with partner proteins. Together, these measurements move beyond observing an abnormal assembly and test how it behaves in cells. This integrated approach supports interpretation of whether aggregation is associated with changes in DISC1 biology.
Localization analysis shows where DISC1 assemblies are found within cells and whether aggregation is associated with a changed cellular distribution. That information is important because DISC1 participates in neuronal signaling and development through its scaffold role. Comparing localization with aggregation measurements can help determine whether altered placement accompanies the formation of oligomers or larger structures.
Cellular models are useful for examining how DISC1 aggregation relates to neuronal functions in a controlled biological setting. Aggregation-targeted interventions can then be evaluated for whether they change aggregation, localization, or binding interactions. These outcomes provide a framework for testing mechanisms relevant to neuropsychiatric disease without treating aggregate formation as an isolated structural observation.