Dataset Information

Structure and interaction dynamics of human proteasome modeled with in-situ cross-links

ABSTRACT: To realize the heterogeneity analysis of the structure and interaction for human 26S proteasomes in the cytoplasm and nucleus, combined with living cell cross-linking and efficient cytoplasm and nucleus separation method, the conformation and interaction resolution of 26S proteasome in the cytoplasm and nucleus was realized. Besides, by ensemble refinement of the interaction conformation of proteasome and ubiquitin with the crosslinking restraints, the transport path of ubiquitin on the proteasome was depicted in the cytoplasm and nucleus. It is of great significance for gaining an intensive understanding of the ubiquitin proteasome system for degrading proteins in the cytoplasm and nucleus.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Lihua Zhang

PROVIDER: PXD042703 | JPOST Repository | Sat Jun 03 00:00:00 BST 2023

REPOSITORIES: jPOST

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			Action	DRS
	proteasome-cytoplasmic-1.raw	Raw
	proteasome-cytoplasmic-2.raw	Raw
	proteasome-cytoplasmic-3.raw	Raw
	proteasome-cytoplasmic-cx-F1-1.raw	Raw
	proteasome-cytoplasmic-cx-F1-2.raw	Raw

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Project description:Sneppen2009 - Modeling proteasome dynamics in Parkinson's disease This model is described in the article: Modeling proteasome dynamics in Parkinson's disease. Sneppen K, Lizana L, Jensen MH, Pigolotti S, Otzen D. Phys Biol 2009; 6(3): 036005 Abstract: In Parkinson's disease (PD), there is evidence that alpha-synuclein (alphaSN) aggregation is coupled to dysfunctional or overburdened protein quality control systems, in particular the ubiquitin-proteasome system. Here, we develop a simple dynamical model for the on-going conflict between alphaSN aggregation and the maintenance of a functional proteasome in the healthy cell, based on the premise that proteasomal activity can be titrated out by mature alphaSN fibrils and their protofilament precursors. In the presence of excess proteasomes the cell easily maintains homeostasis. However, when the ratio between the available proteasome and the alphaSN protofilaments is reduced below a threshold level, we predict a collapse of homeostasis and onset of oscillations in the proteasome concentration. Depleted proteasome opens for accumulation of oligomers. Our analysis suggests that the onset of PD is associated with a proteasome population that becomes occupied in periodic degradation of aggregates. This behavior is found to be the general state of a proteasome/chaperone system under pressure, and suggests new interpretations of other diseases where protein aggregation could stress elements of the protein quality control system. This model is hosted on BioModels Database and identified by: BIOMD0000000548. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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Structure and interaction dynamics of human proteasome modeled with in-situ cross-links

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