6hed Citations

Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.

OpenAccess logo Proc Natl Acad Sci U S A 116 534-539 (2019)
Related entries: 6he4, 6he5, 6he7, 6he8, 6he9, 6hea, 6hec

Cited: 43 times
EuropePMC logo PMID: 30559193

Abstract

Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.

Articles - 6hed mentioned but not cited (3)

  1. Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle. Majumder P, Rudack T, Beck F, Danev R, Pfeifer G, Nagy I, Baumeister W. Proc Natl Acad Sci U S A 116 534-539 (2019)
  2. Minimal mechanistic component of HbYX-dependent proteasome activation that reverses impairment by neurodegenerative-associated oligomers. Chuah JJY, Thibaudeau TA, Smith DM. Commun Biol 6 725 (2023)
  3. research-article Minimal mechanistic component of HbYX-dependent proteasome activation. Chuah JJ, Thibaudeau TA, Rexroad MS, Smith DM. Res Sq rs.3.rs-2496767 (2023)


Reviews citing this publication (12)

  1. The molecular principles governing the activity and functional diversity of AAA+ proteins. Puchades C, Sandate CR, Lander GC. Nat Rev Mol Cell Biol 21 43-58 (2020)
  2. The pre-synaptic fusion machinery. Brunger AT, Choi UB, Lai Y, Leitz J, White KI, Zhou Q. Curr Opin Struct Biol 54 179-188 (2019)
  3. The Proteasome and Its Network: Engineering for Adaptability. Finley D, Prado MA. Cold Spring Harb Perspect Biol 12 a033985 (2020)
  4. Structure, Dynamics and Function of the 26S Proteasome. Mao Y. Subcell Biochem 96 1-151 (2021)
  5. Proteasome in action: substrate degradation by the 26S proteasome. Sahu I, Glickman MH. Biochem Soc Trans 49 629-644 (2021)
  6. Structural Insights into Substrate Recognition and Processing by the 20S Proteasome. Sahu I, Glickman MH. Biomolecules 11 148 (2021)
  7. AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms. Zhang S, Mao Y. Biomolecules 10 E629 (2020)
  8. AAA+ ATPases: structural insertions under the magnifying glass. Jessop M, Felix J, Gutsche I. Curr Opin Struct Biol 66 119-128 (2021)
  9. Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules. Mabanglo MF, Houry WA. J Biol Chem 298 101781 (2022)
  10. Targeting Proteasomes in Cancer and Infectious Disease: A Parallel Strategy to Treat Malignancies and Microbes. Ignatz-Hoover JJ, Murphy EV, Driscoll JJ. Front Cell Infect Microbiol 12 925804 (2022)
  11. Bortezomib advanced mechanisms of action in multiple myeloma, solid and liquid tumors along with its novel therapeutic applications. Alwahsh M, Farhat J, Talhouni S, Hamadneh L, Hergenröder R. EXCLI J 22 146-168 (2023)
  12. A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors. Ye X, Mayne L, Englander SW. J Biol Chem 297 101066 (2021)

Articles citing this publication (28)