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Biology subjects

Lenka, D. R.

Publications and source records attributed to Lenka, D. R..

3 recordsLinked to original sources

A Functional Genetic Atlas of Parkin Resolves Variants of Uncertain Significance and Predicts Parkinson's Disease Age at Onset

Autosomal recessive mutations in the Parkin gene (PRKN) cause early-onset Parkinsons disease (PD). Parkin functions as a ubiquitin E3 ligase acting downstream of the PINK1 kinase to promote phosphorylated ubiquitin at sites of mitochondrial damage. Yet the functional effects of most PRKN gene variants remain unknown. Here we use a pooled cellular assay measuring phosphorylated ubiquitin accumulation to quantify the activity of [~]9,200 PRKN missense and nonsense variants. Our screen identifies thousands of loss- and gain-of-function variants, including activating variants mainly residing at autoinhibitory interfaces. Functional scores accurately distinguish known PD pathogenic and benign variants, and enable reclassification of 173/184 variants of uncertain significance (VUS). When combined into biallelic genotype scores, these data predict the age at disease onset in patients, revealing a quantitative link between Parkin activity and clinical manifestation. Our results provide a comprehensive functional genetic map of Parkin and demonstrate the power of multiplexed assays of variant effects (MAVEs) for variant interpretation and precision medicine in PD.

genetics↗

ISGylation Mechanism Uncovers Conformational Specificity for HECT-family E3 ligase

Interferon-stimulated gene 15 (ISG15), composed of N-terminal and C-terminal ubiquitin-like domains (NTD/CTD), plays a critical role in antiviral immunity. Although the ubiquitination mechanism is well established, the mechanisms governing ISG15 transfer, particularly from E2 to E3 and subsequent lysine conjugation, remain unknown. Here, we reveal that UbcH8(E2)[~]ISG15 exhibits striking specificity for HECT-family E3 ligases (particularly HERC5) but is inactive with RING or RBR E3. In contrast, UbcH8[~]Ub preferentially engages RBR E3, indicating a switched E2-E3 specificity depending on the conjugated ubiquitin-like modifier. Structural and biochemical studies uncover how a unique closed conformation of UbcH8[~]ISG15 enables trans-thiolation mediated by selective HECT-family E3 ligases. We further demonstrate that HERC5s C-lobe specifically recognizes donor ISG15 for lysine conjugation, explaining its exclusive ISGylation activity and lack of ubiquitination function. These findings delineate the molecular basis of ISG15 conjugation and reveal how its pathway has evolved distinct mechanisms from ubiquitination, offering new avenues for therapeutic intervention in infection and immunity.

biophysics↗

Intricate mechanism (s) of substrate specificity and loss of function on disease mutation (K211N) of Parkin

PINK1 and Parkin mutations lead to the early onset of Parkinsons disease. PINK1-mediated phosphorylation of its substrates such as ubiquitin (Ub), ubiquitin-like protein (NEDD8), and ubiquitin-like (Ubl) domain of Parkin activate autoinhibited Parkin E3 ligase. The mechanism of various phospho-Ubls binding on Parkin and conformational changes leading to Parkin activation remain elusive. Herein, we determine the first crystal structure of human Parkin E3 ligase bound with phospho (p)-NEDD8, which shows that NEDD8 has evolved over Ub to bind and activate Parkin more robustly. X-ray crystal structures and supporting biophysical/biochemical data reveal specific recognition and underlying mechanisms of pUb/pNEDD8 and pUbl domain binding to the RING1 and RING0 domains, respectively. This new data also shows that pUb/pNEDD8 binding in the RING1 pocket causes allosteric conformational changes in Parkins catalytic domain (RING2), leading to Parkin activation. Furthermore, Parkinsons disease mutation K211N in the RING0 domain of Parkin was believed to lose its activation due to loss of interaction with pUb. However, our data reveal allosteric conformational changes due to N211 that lock RING2 with RING0 to inhibit Parkin K211N activity without disrupting pNEDD8/pUb binding. This study would aid the design of small-molecule Parkin activators for the treatment of Parkinsons disease.

biochemistry↗