date: 2014-08-06T09:36:45Z
pdf:PDFVersion: 1.4
pdf:docinfo:title: Emerging Mechanistic Insights into AAA Complexes Regulating Proteasomal Degradation
xmp:CreatorTool: PScript5.dll Version 5.2.2
access_permission:can_print_degraded: true
subject: The 26S proteasome is an integral element of the ubiquitin-proteasome system (UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells. It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates. The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases, shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship. Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).
dc:format: application/pdf; version=1.4
pdf:docinfo:creator_tool: PScript5.dll Version 5.2.2
access_permission:fill_in_form: true
pdf:encrypted: false
dc:title: Emerging Mechanistic Insights into AAA Complexes Regulating Proteasomal Degradation
modified: 2014-08-06T09:36:45Z
cp:subject: The 26S proteasome is an integral element of the ubiquitin-proteasome system (UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells. It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates. The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases, shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship. Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).
pdf:docinfo:subject: The 26S proteasome is an integral element of the ubiquitin-proteasome system (UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells. It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates. The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases, shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship. Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).
pdf:docinfo:creator: Friedrich Förster, Jan M. Schuller, Pia Unverdorben, Antje Aufderheide
meta:author: Friedrich Förster, Jan M. Schuller, Pia Unverdorben, Antje Aufderheide
meta:creation-date: 2014-08-06T09:34:45Z
created: 2014-08-06T09:34:45Z
access_permission:extract_for_accessibility: true
Creation-Date: 2014-08-06T09:34:45Z
Author: Friedrich Förster, Jan M. Schuller, Pia Unverdorben, Antje Aufderheide
producer: Acrobat Distiller 9.5.5 (Windows)
pdf:docinfo:producer: Acrobat Distiller 9.5.5 (Windows)
pdf:unmappedUnicodeCharsPerPage: 0
dc:description: The 26S proteasome is an integral element of the ubiquitin-proteasome system (UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells. It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates. The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases, shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship. Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).
Keywords: AAA-ATPases; 26S proteasome; Cdc48; p97; unfoldase; segregase; cryo-EM
access_permission:modify_annotations: true
dc:creator: Friedrich Förster, Jan M. Schuller, Pia Unverdorben, Antje Aufderheide
description: The 26S proteasome is an integral element of the ubiquitin-proteasome system (UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells. It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates. The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases, shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship. Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).
dcterms:created: 2014-08-06T09:34:45Z
Last-Modified: 2014-08-06T09:36:45Z
dcterms:modified: 2014-08-06T09:36:45Z
title: Emerging Mechanistic Insights into AAA Complexes Regulating Proteasomal Degradation
xmpMM:DocumentID: uuid:70f087e1-9080-456d-8c44-0f3ba54a5790
Last-Save-Date: 2014-08-06T09:36:45Z
pdf:docinfo:keywords: AAA-ATPases; 26S proteasome; Cdc48; p97; unfoldase; segregase; cryo-EM
pdf:docinfo:modified: 2014-08-06T09:36:45Z
meta:save-date: 2014-08-06T09:36:45Z
Content-Type: application/pdf
X-Parsed-By: org.apache.tika.parser.DefaultParser
creator: Friedrich Förster, Jan M. Schuller, Pia Unverdorben, Antje Aufderheide
dc:subject: AAA-ATPases; 26S proteasome; Cdc48; p97; unfoldase; segregase; cryo-EM
access_permission:assemble_document: true
xmpTPg:NPages: 21
pdf:charsPerPage: 2353
access_permission:extract_content: true
access_permission:can_print: true
meta:keyword: AAA-ATPases; 26S proteasome; Cdc48; p97; unfoldase; segregase; cryo-EM
access_permission:can_modify: true
pdf:docinfo:created: 2014-08-06T09:34:45Z