A5092174092- Ubiquitin and proteasome pathways
- Protein Degradation and Inhibitors
- Parkinson's Disease Mechanisms and Treatments
- Autophagy in Disease and Therapy
- Cellular transport and secretion
- Histone Deacetylase Inhibitors Research
Indian Institute of Science Education and Research, Bhopal
2023-2024
Loss-of-function Parkin mutations lead to early-onset of Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation its ubiquitin-like (Ubl) domain and the PINK1 kinase. Herein, we demonstrate a competitive binding phospho-Ubl RING2 domains towards RING0 domain, which regulates activity. We show that phosphorylated can complex with native Parkin, leading activation autoinhibited in trans . Furthermore, activator element (ACT) required maintain enzyme...
Loss-of-function Parkin mutations lead to early-onset of Parkinson's disease. is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation its ubiquitin-like (Ubl) domain and the PINK1 kinase. Herein, we demonstrate a competitive binding phospho-Ubl RING2 domains towards RING0 domain, which regulates activity. We show that phosphorylated can complex with native Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain enzyme...
<title>Abstract</title> Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3-ligase activated by phosphorylation its ubiquitin-like (Ubl) domain and PINK1. Herein, we show a competitive binding mode the phospho-Ubl RING2 domains on RING0 domain, which regulates activity. We that phosphorylated can complex with unmodified Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain enzyme’s...
<title>Abstract</title> Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by phosphorylation its ubiquitin-like (Ubl) domain and PINK1. Herein, we show a competitive binding mode the phospho-Ubl RING2 domains on RING0 domain, which regulates activity. We that phosphorylated can directly complex with unmodified Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain...
<title>Abstract</title> Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by phosphorylation its ubiquitin-like (Ubl) domain and PINK1. Herein, we show a competitive binding mode the phospho-Ubl RING2 domains on RING0 domain, which regulates activity. We that phosphorylated can directly complex with unmodified Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain...
Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by phosphorylation its ubiquitin-like (Ubl) domain and PINK1. Herein, we show a competitive binding mode the phospho-Ubl RING2 domains on RING0 domain, which regulates activity. We that phosphorylated can directly complex with unmodified Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain enzyme’s kinetics, removal...
<title>Abstract</title> Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation its ubiquitin-like (Ubl) domain and the PINK1 kinase. Herein, we demonstrate a competitive binding phospho-Ubl RING2 domains towards RING0 domain, which regulates activity. We show that phosphorylated can complex with native Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required...
Loss of function Parkin mutations lead to early-onset Parkinson’s disease. is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation its ubiquitin-like (Ubl) domain and the PINK1 kinase. Herein, we demonstrate a competitive binding phospho-Ubl RING2 domains towards RING0 domain, which regulates activity. We show that phosphorylated can complex with native Parkin, leading activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain enzyme...
<title>Abstract</title> Parkin E3-ligase is an auto-inhibited enzyme activated by phosphorylation of ubiquitin or ubiquitin-like (Ubl) domain parkin PINK1. mutations are known to affect its function leading the onset Parkinson’s disease. Herein, we show a competitive binding mode phospho-Ubl and RING2 domains on RING0 domain, which regulates activity. We that phosphorylated forms complex with native activation autoinhibited in trans. Furthermore, activator element (ACT) required maintain...