☆ 4.8 Editorial Material

Hsm3/S5b Joins the Ranks of 26S Proteasome Assembly Chaperones

MOLECULAR CELL (2009)

Journal

MOLECULAR CELL

Volume 33, Issue 4, Pages 415-416

Publisher

CELL PRESS

DOI: 10.1016/j.molcel.2009.02.007

Keywords

-

Categories

Biochemistry & Molecular Biology Cell Biology

Ask authors/readers for more resources

Protocol

Community support

Reagent

Community support

Abstract

In a recent issue of Molecular Cell, Le Tallec et al. (2009) characterize the yeast Hsm3 protein, an apparent ortholog of human S5b, as a dedicated chaperone that promotes assembly of the base subcomplex of the 19S proteasome activator.

Authors

I am an author on this paper

Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8

Not enough ratings

Secondary Ratings

Novelty

-

Significance

-

Scientific rigor

-

Rate this paper

Recommended

Article Biochemistry & Molecular Biology

Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly

Ana C. Matias, Joao Matos, R. Juergen Dohmen, Paula C. Ramos

Summary: While assembly of the 20S proteasome core particle (CP) in prokaryotes occurs spontaneously, in eukaryotes, dedicated assembly chaperones are required for efficient CP assembly. This study found that in S. cerevisiae, the CP subunits alpha 1, alpha 2, and alpha 4 form independent small complexes instead of a complete alpha-ring. The presence of Hsp70 and Hsp110 chaperones was detected in these complexes, and they were found to cooperate in promoting the folding and assembly of alpha subunits with other CP subunits.

BIOMOLECULES (2023)

Add to Collection

Article Chemistry, Physical

Stability of 20S Proteasome Configurations: Preopening the Axial Gate

Lucas W. Henderson, Edie M. Sharon, Amit K. S. Gautam, Adam J. Anthony, Martin F. Jarrold, David H. Russell, Andreas Matouschek, David E. Clemmer

Summary: Mass spectrometry studies show that the stability of S. cerevisiae 20S proteasome undergoes related configurations and transitions during temperature changes, possibly linked to the opening of the proteolytic core. The study indicates that the proteasome remains intact and all transitions are reversible. Three types of structures are identified based on thermodynamic analysis: energetically stabilized closed configurations, high-entropy precursor states, and open pore structures. Opening of the 20S pore in the absence of the regulatory unit involves a charge-priming process. However, only a small fraction of precursor configurations actually open to expose the catalytic cavity.

JOURNAL OF PHYSICAL CHEMISTRY LETTERS (2023)

Add to Collection

Article Biochemistry & Molecular Biology

Metformin Induces Resistance of Cancer Cells to the Proteasome Inhibitor Bortezomib

Camille Schlesser, Thomas Meul, Georgios Stathopoulos, Silke Meiners

Summary: The anti-diabetic drug metformin induces resistance of cancer cells to the proteasome inhibitor Bortezomib by impairing the activity and assembly of the 26S proteasome complexes.

BIOMOLECULES (2022)

Add to Collection

Article Multidisciplinary Sciences

Deubiquitination of proteasome subunits by OTULIN regulates type I IFN production

Panfeng Tao, Shihao Wang, Seza Ozen, Pui Y. Lee, Jiahui Zhang, Jun Wang, Huan Han, Zhaohui Yang, Ran Fang, Wanxia Li Tsai, Huanming Yang, Erdal Sag, Rezan Topaloglu, Ivona Aksentijevich, Xiaomin Yu, Qing Zhou

Summary: OTULIN deficiency leads to activation of NF-κB and IFN-I signaling pathways, caused by dysregulated proteasomes due to the deubiquitinase activity of OTULIN. This suggests a crucial role of linear ubiquitination in regulating proteasome function and its link to autoinflammatory syndromes associated with proteasome dysfunction.

SCIENCE ADVANCES (2021)

Add to Collection

Review Plant Sciences

The Ubiquitin-Proteasome System (UPS) and Viral Infection in Plants

Dania P. Lobaina, Roberto Tarazi, Tamara Castorino, Maite F. S. Vaslin

Summary: The ubiquitin-proteasome system (UPS) is crucial for maintaining cellular balance and plays a key role in DNA repair, gene transcription, and protein activation. Viruses often manipulate the UPS to maintain viral protein levels and evade host defenses. Understanding the mechanisms used by plant viruses to subvert host defenses is important for developing biotechnological approaches for viral resistance.

PLANTS-BASEL (2022)

Add to Collection

Article Biochemistry & Molecular Biology

The penultimate step of proteasomal ATPase assembly is mediated by a switch dependent on the chaperone Nas2

Suganya Sekaran, Soyeon Park

Summary: The proteasome holoenzyme is a complex molecular machine that degrades most proteins. The assembly of the heterohexameric Rpt ring, a crucial part of the proteasome holoenzyme, is regulated by the release of a specific chaperone, Nas2, which ensures proper Rpt ring assembly. Nas2 acts by blocking premature progression of the assembly and can activate an assembly checkpoint to ensure the composition and functional competence of the proteasomal ATPase. This study provides insights into the mechanisms involved in the assembly of the proteasome holoenzyme.

JOURNAL OF BIOLOGICAL CHEMISTRY (2023)

Add to Collection

Article Biochemistry & Molecular Biology

Conserved proline residues in the coiled coil-OB domain linkers of Rpt proteins facilitate eukaryotic proteasome base assembly

Chin Leng Cheng, Michael K. Wong, Yanjie Li, Mark Hochstrasser

Summary: The study reveals the importance of proline residues in the proteasome-activating nucleotidase for efficient assembly of the 26S proteasome base in eukaryotes and archaea. Investigation of equivalent prolines in Rpt2, Rpt3, and Rpt5 suggests their crucial role in specific ATPase heterodimerization during proteasome base assembly.

JOURNAL OF BIOLOGICAL CHEMISTRY (2021)

Add to Collection

Article Biochemistry & Molecular Biology

PKR Protects the Major Catalytic Subunit of PKA Cpk1 from FgBlm10-Mediated Proteasome Degradation in Fusarium graminearum

Chen Gong, Daiying Xu, Daiyuan Sun, Xue Zhang

Summary: The degradation of the proteasome core subunit Cpk1 is protected by Pkr. Mutations in the FgBlm10 C-terminus, PRE6 ortholog (FGRRES_07282), and PRE5 ortholog (FGRRES_05222) were found to rescue defects in growth, conidial morphology, Cpk1 stability, and PKA activities in the pkr mutant. The interaction between FgBlm10 and FgPre5/FgPre6 was detected, and key elements for their interaction were characterized. PKA indirectly affects the phosphorylation and localization of FgBlm10, and truncation of its C-terminus enhances nuclear import and bleomycin resistance.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)

Add to Collection

Review Biochemistry & Molecular Biology

The Ubiquitin-26S Proteasome Pathway and Its Role in the Ripening of Fleshy Fruits

Wen Jia, Gangshuai Liu, Peiyu Zhang, Hongli Li, Zhenzhen Peng, Yunxiang Wang, Tomislav Jemric, Daqi Fu

Summary: The 26S proteasome is an ATP-dependent proteolytic complex that degrades damaged and misfolded proteins, as well as regulatory proteins in eukaryotic cells, playing a crucial role in maintaining protein homeostasis. The ubiquitin-26S proteasome pathway is a post-translational regulatory mechanism that targets a wide range of protein substrates in plants, involved in various stages of plant growth and development, and fruit ripening. This paper reviews the structure and mechanism of the 26S proteasome and the function of the ubiquitin-26S proteasome pathway in the ripening process of fleshy fruits.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2023)

Add to Collection

Article Multidisciplinary Sciences

Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores

Nathan Jespersen, Kai Ehrenbolger, Rahel R. Winiger, Dennis Svedberg, Charles R. Vossbrinck, Jonas Barandun

Summary: The structure and complexity of proteasomes in microsporidia vary between dormant and germinated stages, with highly derived structures that can be targeted for development of specific inhibitors. The findings shed light on the unique evolution and biology of these medically and economically important pathogens.

NATURE COMMUNICATIONS (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Proteasome inhibition alters mitotic progression through the upregulation of centromeric alpha-Satellite RNAs

Rodrigo E. Caceres-Gutierrez, Marco A. Andonegui, Diego A. Oliva-Rico, Rodrigo Gonzalez-Barrios, Fernando Luna, Cristian Arriaga-Canon, Alejandro Lopez-Saavedra, Diddier Prada, Clementina Castro, Laurent Parmentier, Jose Diaz-Chavez, Yair Alfaro-Mora, Erick Navarro-Delgado, Eunice Fabian-Morales, Bao Tran, Jyoti Shetty, Yongmei Zhao, Nicolas Alcaraz, Carlos De la Rosa, Jose L. Reyes, Sabrine Hedouin, Florent Hube, Claire Francastel, Luis A. Herrera

Summary: The study reveals that proteasome inhibition leads to upregulation of repetitive RNAs, particularly affecting alpha-Satellite RNAs in cancer cells. The results show fluctuation of alpha-Satellite RNAs along the cell cycle and their interaction with members of the cohesin ring, suggesting a role in mitotic progression regulation.

FEBS JOURNAL (2022)

Add to Collection

Article Nutrition & Dietetics

Changes in Skeletal Muscle Protein Metabolism Signaling Induced by Glutamine Supplementation and Exercise

Carlos Flores Rodrigues Jr, Gilson Masahiro Murata, Frederico Gerlinger-Romero, Renato Tadeu Nachbar, Gabriel Nasri Marzuca-Nassr, Renata Gorjao, Kaio Fernando Vitzel, Sandro Massao Hirabara, Tania Cristina Pithon-Curi, Rui Curi

Summary: Resistance exercise training (RET) and glutamine supplementation (GS) can increase muscle cross-sectional area (CSA) in adult rats by upregulating phosphorylation of signaling proteins.

NUTRIENTS (2023)

Add to Collection

Article Biology

High resolution structures define divergent and convergent mechanisms of archaeal proteasome activation

Janelle J. Y. Chuah, Matthew S. Rexroad, David M. Smith

Summary: Considering the link between neurodegenerative diseases and impaired proteasome function, it's crucial to understand proteasome activation mechanisms. Our study investigates the allosteric mechanism of gate-opening in the archaeal proteasome using a mimetic of the HbYX motif. We propose a detailed molecular model for HbYX-dependent 20S gate-opening, enabling the development of small molecule proteasome activators for treating neurodegenerative diseases.

COMMUNICATIONS BIOLOGY (2023)

Add to Collection

Article Biochemical Research Methods

Enabling Photoactivated Cross-Linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-Cleavable Cross-Linkers

Craig Gutierrez, Leah J. Salituro, Clinton Yu, Xiaorong Wang, Sadie F. DePeter, Scott D. Rychnovsky, Lan Huang

Summary: XL-MS is a powerful tool for studying protein-protein interactions and elucidating architectures of protein complexes. The development of novel MS-cleavable heterobifunctional cross-linkers, such as SDASO, enables fast and accurate identification of photocross-linked peptides by MSn. The feasibility of photocross-linking large protein complexes has been demonstrated, laying the foundation for future applications in complex XL-MS studies.

MOLECULAR & CELLULAR PROTEOMICS (2021)

Add to Collection

Article Biochemical Research Methods

CRISPR/Cas9-Mediated Genome Engineering Reveals the Contribution of the 26S Proteasome to the Extremophilic Nature of the Yeast Debaryomyces hansenii

Daria S. Spasskaya, Mikhail Kotlov, Dmitriy S. Lekanov, Vera V. Tutyaeva, Anastasiya Snezhkina, Anna Kudryavtseva, Vadim L. Karpov, Dmitry S. Karpov

Summary: Debaryomyces hansenii is a marine yeast of high importance in various industries and a popular model for studying halo- and osmotolerance mechanisms. The developed CRISPR systems allow efficient genome engineering in D. hansenii, providing a genetic approach to control proteasome activity and advancing applications of this yeast.

ACS SYNTHETIC BIOLOGY (2021)

Add to Collection

Editorial Material Cell Biology

Comment on: Gonzalez-Prieto R, et al. c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4. Cell Cycle 2015; 14(12):1859-72; PMID: 25895136; http://dx.doi.org/10.1080/15384101.2015.1040965

R. Juergen Dohmen

CELL CYCLE (2015)

Add to Collection

Article Biochemistry & Molecular Biology

In Vitro Studies Reveal a Sequential Mode of Chain Processing by the Yeast SUMO (Small Ubiquitin-related Modifier)-specific Protease Ulp2

Julia Eckhoff, R. Juergen Dohmen

JOURNAL OF BIOLOGICAL CHEMISTRY (2015)

Add to Collection

Article Multidisciplinary Sciences

Proteasome assembly from 15S precursors involves major conformational changes and recycling of the Pba1-Pba2 chaperone

Malte Kock, Maria M. Nunes, Matthias Hemann, Sebastian Kube, R. Juergen Dohmen, Franz Herzog, Paula C. Ramos, Petra Wendler

NATURE COMMUNICATIONS (2015)

Add to Collection

Article Multidisciplinary Sciences

Phenotypes on demand via switchable target protein degradation in multicellular organisms

Frederik Faden, Thomas Ramezani, Stefan Mielke, Isabel Almudi, Knud Nairz, Marceli S. Froehlich, Joerg Hoeckendorff, Wolfgang Brandt, Wolfgang Hoehenwarter, R. Juergen Dohmen, Arp Schnittger, Nico Dissmeyer

Nature Communications (2016)

Add to Collection

Article Biochemistry & Molecular Biology

Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO

Kirstin Keusekotten, Veronika N. Bade, Katrin Meyer-Teschendorf, Annie Miriam Sriramachandran, Katrin Fischer-Schrader, Anke Krause, Christiane Horst, Guenter Schwarz, Kay Hofmann, R. Juergen Dohmen, Gerrit J. K. Praefcke

BIOCHEMICAL JOURNAL (2014)

Add to Collection

Review Biochemistry & Molecular Biology

SUMO-targeted ubiquitin ligases

Annie M. Sriramachandran, R. Juergen Dohmen

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2014)

Add to Collection

Article Biochemistry & Molecular Biology

A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway

Bebiana Sa-Moura, Minoru Funakoshi, Robert J. Tomko, R. Juergen Dohmen, Zhiping Wu, Junmin Peng, Mark Hochstrasser

JOURNAL OF BIOLOGICAL CHEMISTRY (2013)

Add to Collection

Article Multidisciplinary Sciences

Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain

Annie M. Sriramachandran, Katrin Meyer-Teschendorf, Stefan Pabst, Helle D. Ulrich, Niels H. Gehring, Kay Hofmann, Gerrit J. K. Praefcke, R. Jurgen Dohmen

NATURE COMMUNICATIONS (2019)

Add to Collection

Article Biochemistry & Molecular Biology

Ribosome-associated quality control mediates degradation of the premature translation termination product Orf1p of ODC antizyme mRNA

Ashis Kumar Pradhan, Ganapathi Kandasamy, Upasana Chatterjee, Anushree Bharadwaj, Sam J. Mathew, R. Jurgen Dohmen, R. Palanimurugan

Summary: This study reveals that the degradation of Orf1p requires the coordinated action of both ribosome-associated and cytosolic protein quality control factors.

FEBS LETTERS (2021)

Add to Collection

Letter Immunology

Curative Treatment of POMP-Related Autoinflammation and Immune Dysregulation (PRAID) by Hematopoietic Stem Cell Transplantation

Andrea Meinhardt, Paula C. Ramos, R. Juergen Dohmen, Nadja Lucas, Min Ae Lee-Kirsch, Benjamin Becker, Jan de Laffolie, Tomas Cunha, Tim Niehues, Ulrich Salzer, Ayami Yoshimi, Miriam Erlacher, Anke M. J. Peters, Stephan Ehl, Brigitte Strahm, Carsten Speckmann

JOURNAL OF CLINICAL IMMUNOLOGY (2021)

Add to Collection

Article Biochemistry & Molecular Biology

Interaction with the Assembly Chaperone Ump1 Promotes Incorporation of the β7 Subunit into Half-Proteasome Precursor Complexes Driving Their Dimerization

Jessica Zimmermann, Paula C. Ramos, R. Juergen Dohmen

Summary: This study elucidates the important interaction between Ump1 and the β7 subunit, which is crucial for the biogenesis of the proteasome core particle.

BIOMOLECULES (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Hypusinated eIF5A Promotes Ribosomal Frameshifting during Decoding of ODC Antizyme mRNA in Saccharomyces cerevisiae

Kai Halwas, Lennard-Maximilian Doering, Franziska Valentina Oehlert, R. Juergen Dohmen

Summary: Polyamines are important biogenic polycations that play essential roles in various cellular processes and diseases. The biosynthesis of polyamines involves the conversion of ornithine to putrescine by ornithine decarboxylase (ODC). The regulation of ODC by ODC antizyme (OAZ) involves a unique mechanism of posttranslational regulation through polyamine-regulated bypassing of an internal translation termination codon. The depletion of polyamines inhibits translation across the OAZ1 ribosomal frameshift (RFS) site by affecting eIF5A hypusination and RFS directly.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly

Ana C. Matias, Joao Matos, R. Juergen Dohmen, Paula C. Ramos

Summary: While assembly of the 20S proteasome core particle (CP) in prokaryotes occurs spontaneously, in eukaryotes, dedicated assembly chaperones are required for efficient CP assembly. This study found that in S. cerevisiae, the CP subunits alpha 1, alpha 2, and alpha 4 form independent small complexes instead of a complete alpha-ring. The presence of Hsp70 and Hsp110 chaperones was detected in these complexes, and they were found to cooperate in promoting the folding and assembly of alpha subunits with other CP subunits.

BIOMOLECULES (2023)

Add to Collection

Article Cell Biology

Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome

R. Roshini Beenukumar, Daniela Godderz, R. Palanimurugan, R. Juergen Dohmen

MICROBIAL CELL (2015)

Add to Collection

Article Biology

Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation

Ramona Schuster, Vincent Anton, Tania Simoes, Selver Altin, Fabian den Brave, Thomas Hermanns, Manuela Hospenthal, David Komander, Gunnar Dittmar, R. Juergen Dohmen, Mafalda Escobar-Henriques

LIFE SCIENCE ALLIANCE (2020)

Add to Collection

No Data Available

© Peeref 2019-2024. All rights reserved.