Unlocking the electrochemical functions of biomolecular condensates
Biomolecular condensation is a key mechanism for organizing cellular processes in a
spatiotemporal manner. The phase-transition nature of this process defines a density …
spatiotemporal manner. The phase-transition nature of this process defines a density …
Phase separation of microtubule-binding proteins–implications for neuronal function and disease
D Duan, AJ Koleske - Journal of Cell Science, 2024 - journals.biologists.com
Protein liquid–liquid phase separation (LLPS) is driven by intrinsically disordered regions
and multivalent binding domains, both of which are common features of diverse microtubule …
and multivalent binding domains, both of which are common features of diverse microtubule …
Biomolecular condensates can function as inherent catalysts
We report the discovery that chemical reactions such as ATP hydrolysis can be catalyzed by
condensates formed by intrinsically disordered proteins (IDPs), which themselves lack any …
condensates formed by intrinsically disordered proteins (IDPs), which themselves lack any …
Structural details of helix-mediated TDP-43 C-terminal domain multimerization
The primarily disordered C-terminal domain (CTD) of TAR DNA binding protein-43 (TDP-
43), a key nuclear protein in RNA metabolism, forms neuronal inclusions in several …
43), a key nuclear protein in RNA metabolism, forms neuronal inclusions in several …
[HTML][HTML] C9orf72 poly-PR forms anisotropic condensates causative of nuclear TDP-43 pathology
RE Hodgson, JA Rayment, WP Huang, AS Avila… - Iscience, 2024 - cell.com
Proteinaceous inclusions formed by C9orf72-derived dipeptide-repeat (DPR) proteins are a
histopathological hallmark in∼ 50% of familial amyotrophic lateral sclerosis/frontotemporal …
histopathological hallmark in∼ 50% of familial amyotrophic lateral sclerosis/frontotemporal …
Molecular simulations of enzymatic phosphorylation of disordered proteins and their condensates
Understanding the condensation and aggregation of intrinsically disordered proteins in a
non-equilibrium environment is crucial for unraveling many biological processes. Active …
non-equilibrium environment is crucial for unraveling many biological processes. Active …
Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution
RF Berkeley, AP Plonski, T Phan, K Grohe, L Becker… - bioRxiv, 2024 - biorxiv.org
Small heat shock proteins (sHSPs), including HSPB1, are essential regulators of cellular
proteostasis that interact with unfolded and partially folded proteins to prevent aberrant …
proteostasis that interact with unfolded and partially folded proteins to prevent aberrant …
Organization of the Proteostasis Network of Membraneless Organelles
Membraneless organelles (MLOs) are dynamic macromolecular condensates that act as
crucibles to modulate biological process within the cell. Since MLOs form in the absence of …
crucibles to modulate biological process within the cell. Since MLOs form in the absence of …
Opto-controlled C9orf72 poly-PR forms anisotropic condensates causative of TDP-43 pathology in the nucleus
RE Hodgson, J Rayment, WP Huang, AS Avila… - bioRxiv, 2024 - biorxiv.org
Proteinaceous inclusions formed by C9orf72 derived dipeptide-repeat (DPR) proteins are a
histopathological hallmark in~ 50% of familial amyotrophic lateral sclerosis/frontotemporal …
histopathological hallmark in~ 50% of familial amyotrophic lateral sclerosis/frontotemporal …
RNA-binding tunes the conformational plasticity and intradomain stability of TDP-43 tandem RNA recognition motifs
TAR DNA binding protein 43 (TDP-43) is a nuclear RNA/DNA-binding protein with pivotal
roles in RNA-related processes such as splicing, transcription, transport, and stability. The …
roles in RNA-related processes such as splicing, transcription, transport, and stability. The …