日本語
 
User Manual Privacy Policy ポリシー/免責事項 連絡先
  詳細検索ブラウズ

アイテム詳細


公開

学術論文

Emerging mechanistic insights into AAA complexes regulating proteasomal degradation.

MPS-Authors
/persons/resource/persons77965

Förster,  Friedrich
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons98592

Schuller,  Jan M.
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78814

Unverdorben,  Pia
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons145201

Aufderheide,  Antje
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

URL
There are no locators available
フルテキスト (公開)

biomolecules-04-00774.pdf
(全文テキスト(全般)), 4MB

付随資料 (公開)
There is no public supplementary material available
引用

Förster, F., Schuller, J. M., Unverdorben, P., & Aufderheide, A. (2014). Emerging mechanistic insights into AAA complexes regulating proteasomal degradation. Biomolecules, 4(3), 774-794. doi:10.3390/biom4030774.


引用: http://hdl.handle.net/11858/00-001M-0000-0025-AF47-5
要旨
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).