Related Experiment Video
Updated: Feb 9, 2026

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
Published on: December 14, 2017
Regulation of LRRK2: insights from structural and biochemical analysis
Bernd K Gilsbach1, Marita Eckert1, Christian Johannes Gloeckner1,2
1DZNE-German Center for Neurodegenerative Diseases, Otfried-Müller Str. 23, D-72076 Tübingen, Germany.
Abstract:
Leucine-rich repeat kinase 2 (LRRK2) is a multi-domain protein and its mutations can lead to Parkinson's disease. Recent studies on LRRK2 and homologue proteins have advanced our mechanistic understanding of LRRK2 regulation. Here, we summarize the available data on the biochemistry and structure of LRRK2 and postulate three possible layers of regulation, translocation, monomer-dimer equilibrium and intramolecular activation of domains.
More Related Videos
12:49Human Peripheral Blood Neutrophil Isolation for Interrogating the Parkinson's Associated LRRK2 Kinase Pathway by Assessing Rab10 Phosphorylation
Published on: March 21, 2020
07:10Author Spotlight: Expression and Purification of Human Solute Carrier Transporters Using Codon-Optimized Genes
Published on: September 29, 2023
Related Concept Videos
Chromatin Structure Regulates pre-mRNA Processing
The chromatin structure, especially...
Epigenetic Regulation
Cooperative Binding of Transcription Regulators
GTPases and their Regulation
Large G-proteins,...
Regulated mRNA Transport
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....