Detection of endogenous S1292 LRRK2 autophosphorylation in mouse tissue as a readout for kinase activity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Jillian H. Kluss, Melissa M. Conti, Alice Kaganovich, Aleksandra Beilina, Heather L. Melrose, Mark R. Cookson, Adamantios Mamais

ABSTRACT

Parkinson's disease-linked mutations in LRRK2 enhance the kinase activity of the protein, therefore targeting LRRK2 kinase activity is a promising therapeutic approach. Phosphorylation at S935 of LRRK2 and of its Rab GTPase substrates have proven very useful biomarkers to monitor its kinase activity. Complementary to these approaches autophosphorylation of LRRK2 can be used as a direct kinase activity readout but to date detection of autophosphorylation at endogenous levels in vivo has been limited. We developed a fractionation-based enrichment method to successfully detect endogenous S1292 LRRK2 autophosphorylation in mouse tissues and highlight S1292 as a physiological readout candidate for LRRK2 kinase activity in vivo. More... »

PAGES

13

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41531-018-0049-1

DOI

http://dx.doi.org/10.1038/s41531-018-0049-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1103479205

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29707617


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