Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation

Biochem Biophys Res Commun. 2013 Nov 29;441(4):862-6. doi: 10.1016/j.bbrc.2013.10.159. Epub 2013 Nov 6.

Abstract

LRRK2 is one of the most important genetic contributors to Parkinson's disease (PD). Point mutations in this gene cause an autosomal dominant form of PD, but to date no cellular phenotype has been consistently linked with mutations in each of the functional domains (ROC, COR and Kinase) of the protein product of this gene. In this study, primary fibroblasts from individuals carrying pathogenic mutations in the three central domains of LRRK2 were assessed for alterations in the autophagy/lysosomal pathway using a combination of biochemical and cellular approaches. Mutations in all three domains resulted in alterations in markers for autophagy/lysosomal function compared to wild type cells. These data highlight the autophagy and lysosomal pathways as read outs for pathogenic LRRK2 function and as a marker for disease, and provide insight into the mechanisms linking LRRK2 function and mutations.

Keywords: Autophagy; C-terminal of ROC; COR; ICC; Immunocytochemistry; LRRK2; Lysosomes; PD; Parkinson’s disease; ROC; Signaling pathways; leucine rich repeat kinase 2; ras of complex proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy / genetics*
  • Catalytic Domain / genetics
  • Cell Culture Techniques
  • Female
  • Fibroblasts
  • Genetic Markers
  • Humans
  • Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
  • Lysosomes / genetics*
  • Male
  • Microtubule-Associated Proteins / metabolism
  • Parkinson Disease / genetics*
  • Parkinson Disease / pathology
  • Point Mutation
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / physiology*
  • Protein Structure, Tertiary

Substances

  • Genetic Markers
  • MAP1LC3A protein, human
  • Microtubule-Associated Proteins
  • LRRK2 protein, human
  • Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
  • Protein Serine-Threonine Kinases