Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains
KA Waite, G Vontz, SY Lee… - Proceedings of the …, 2024 - National Acad Sciences
Stress conditions can cause the relocalization of proteasomes to condensates in yeast and
mammalian cells. The interactions that facilitate the formation of proteasome condensates …
mammalian cells. The interactions that facilitate the formation of proteasome condensates …
Short disordered termini and proline-rich domain are major regulators of UBQLN1/2/4 phase separation
TP Dao, A Rajendran, SKK Galagedera, W Haws… - Biophysical …, 2024 - cell.com
Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2, and UBQLN4
differ in both their specific protein quality control functions and their propensities to localize …
differ in both their specific protein quality control functions and their propensities to localize …
Challenges in bridging the gap between protein structure prediction and functional interpretation
The rapid evolution of protein structure prediction tools has significantly broadened access
to protein structural data. Although predicted structure models have the potential to …
to protein structural data. Although predicted structure models have the potential to …
High-throughput assay exploiting disorder-to-order conformational switches: application to the proteasomal Rpn10: E6AP complex
CS Muli, SG Tarasov, KJ Walters - Chemical science, 2024 - pubs.rsc.org
Conformational switching is pervasively driven by protein interactions, particularly for
intrinsically disordered binding partners. We developed a dually orthogonal fluorescence …
intrinsically disordered binding partners. We developed a dually orthogonal fluorescence …
[HTML][HTML] Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate
IM Valentino, JG Llivicota-Guaman, TP Dao, EO Mulvey… - bioRxiv, 2024 - ncbi.nlm.nih.gov
Ubiquitination is one of the most common post-translational modifications in eukaryotic cells.
Depending on the architecture of polyubiquitin chains, substrate proteins can meet different …
Depending on the architecture of polyubiquitin chains, substrate proteins can meet different …
[HTML][HTML] Short N-terminal disordered regions and the proline-rich domain are major regulators of phase transitions for full-length UBQLN1, UBQLN2 and UBQLN4
TP Dao, A Rajendran, SKK Galagedera, W Haws… - bioRxiv, 2023 - ncbi.nlm.nih.gov
Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2 and UBQLN4 differ
in both their specific protein quality control functions and their propensities to localize to …
in both their specific protein quality control functions and their propensities to localize to …
The structural and biophysical basis of substrate binding to the hydrophobic groove in Ubiquilin Sti1 domains
J Onwunma, S Binsabaan, SP Allen, B Sankaran… - bioRxiv, 2024 - biorxiv.org
Ubiquilins are a family of cytosolic proteins that ferry ubiquitinated substrates to the
proteasome for degradation. Recent work has demonstrated that Ubiquilins can also act as …
proteasome for degradation. Recent work has demonstrated that Ubiquilins can also act as …
E3 ligase recruitment by UBQLN2 protects substrates from proteasomal degradation
A Scheutzow, S Thanthirige, G Siffer, ML Wohlever - bioRxiv, 2024 - biorxiv.org
Ubiquilins are a family of proteins critical to cellular proteostasis that are also linked to
neurodegenerative diseases such as ALS, with specific mutations in UBQLN2 causing …
neurodegenerative diseases such as ALS, with specific mutations in UBQLN2 causing …
[HTML][HTML] We con-dense if we want to; We can't leave AZUL outside
TP Dao, CA Castañeda - Structure, 2023 - Elsevier
In this issue of Structure, Buel et al.(2023) combined NMR data with AlphaFold2 to map out
the interaction between the AZUL domain of ubiquitin ligase E6AP and UBQLN1/2 UBA. The …
the interaction between the AZUL domain of ubiquitin ligase E6AP and UBQLN1/2 UBA. The …
1H, 15N, 13C backbone and Cβ resonance assignments for UBQLN1 UBA and UBAA domains
UBQLN1 functions in autophagy and proteasome-mediated protein degradation. It contains
an N-terminal ubiquitin-like domain (UBL), a C-terminal ubiquitin-associated domain (UBA) …
an N-terminal ubiquitin-like domain (UBL), a C-terminal ubiquitin-associated domain (UBA) …