PXD028941 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Nuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like InclusionsNuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like Inclusions |
Description | Biogenesis of inclusion bodies (IBs) facilitates protein quality control (PQC). Canonical aggresomes execute degradation of misfolded proteins while non-degradable amyloids quarantine into Insoluble Protein Deposits. Lewy Bodies (LBs) are well-known neurodegenerative IBs of α-Synuclein but PQC-benefits and drawbacks associated with LBs remain underexplored. Here, we report that a crosstalk between LBs and aggresome-like IBs of α-Synuclein (Syn-aggresomes) buffer amyloidogenic α-Synuclein load. LBs possess unorthodox PQC-capacities of self-quarantining Syn-amyloids and being degradable upon receding fresh amyloidogenesis. Syn-aggresomes equilibrate biogenesis of LBs by facilitating spontaneous degradation of soluble α-Synuclein and opportunistic turnover of Syn-amyloids. LBs overgrow at the perinucleus once amyloidogenesis sets in and are misidentified by cytosolic BICD2 as cargos for motor-protein dynein. Simultaneously, microtubules surrounding the perinuclear LBs are distorted misbalancing the dynein motor-force on nucleoskeleton leading to widespread lamina injuries. Like typical Laminopathies, nucleocytoplasmic mixing, DNA-damage, and deregulated transcription of stress chaperones defeat the proteostatic purposes of LBs. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:35:13.124.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Swasti Raychaudhuri |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-10-04 10:03:37 | ID requested | |
1 | 2024-04-04 08:25:08 | announced | |
⏵ 2 | 2024-10-22 06:35:13 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1242/jcs.261935; |
Mansuri S, Jain A, Singh R, Rawat S, Mondal D, Raychaudhuri S, -synuclein amyloid inclusions. J Cell Sci, 137(7):(2024) [pubmed] |
Keyword List
submitter keyword: -Synuclein, Syn-aggresomes, Nuclear envelope injury, inclusion bodies, Lewy Body, proteostasis over-saturation |
Contact List
Swasti Raychaudhuri |
contact affiliation | Principal Scientist, CSIR- Centre for Cellular and Molecular Biology, Hyderabad, India |
contact email | rcswasti@ccmb.res.in |
lab head | |
Swasti Raychaudhuri |
contact affiliation | CSIR-Centre for Cellular and Molecular Biology |
contact email | rcswasti@ccmb.res.in |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD028941
- Label: PRIDE project
- Name: Nuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like InclusionsNuclear-injuries by aberrant dynein-forces defeat proteostatic purposes of Lewy Body-like Inclusions