Cargando…
Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations
Missense mutations of the phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) gene cause autosomal-recessive Parkinson's disease. To date, little is known about the intrinsic catalytic properties of PINK1 since the human enzyme displays such low kinase activity in vitro. We have disc...
Autores principales: | Woodroof, Helen I., Pogson, Joe H., Begley, Mike, Cantley, Lewis C., Deak, Maria, Campbell, David G., van Aalten, Daan M. F., Whitworth, Alexander J., Alessi, Dario R., Muqit, Miratul M. K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3352081/ https://www.ncbi.nlm.nih.gov/pubmed/22645651 http://dx.doi.org/10.1098/rsob.110012 |
Ejemplares similares
-
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations
por: Kumar, Atul, et al.
Publicado: (2017) -
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
por: Kondapalli, Chandana, et al.
Publicado: (2012) -
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser(65)
por: Kazlauskaite, Agne, et al.
Publicado: (2014) -
PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease
por: Kazlauskaite, Agne, et al.
Publicado: (2015) -
Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation
por: Kazlauskaite, Agne, et al.
Publicado: (2015)