Identification of bona-fide LRRK2 kinase substrates

Movement Disorders

Volumn 31, Issue 8, 2016, Pages 1140-1141

  West, Andrew B ^a   Cookson, Mark R ^b  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b NATIONAL INSTITUTE ON AGING   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; LEUCINE RICH REPEAT KINASE 2; PHOSPHOPEPTIDE; RAB PROTEIN; RAB10 PROTEIN; RAB8 PROTEIN; UNCLASSIFIED DRUG; PROTEIN SERINE THREONINE KINASE;

AUTOPHOSPHORYLATION; EDITORIAL; ENZYME ACTIVITY; ENZYME SUBSTRATE; GENE; GENE MUTATION; GENETIC SUSCEPTIBILITY; HUMAN; LRRK2 GENE; NERVE DEGENERATION; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION;

LEUCINE-RICH REPEAT SERINE-THREONINE PROTEIN KINASE-2; PARKINSON DISEASE; PROTEIN-SERINE-THREONINE KINASES;

EID: 84981164616     PISSN: 08853185     EISSN: 15318257     Source Type: Journal    
DOI: 10.1002/mds.26647     Document Type: Editorial

References (5)

1. West AB, Moore DJ, Biskup S, et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc Natl Acad Sci U S A 2005;102:16842-16847.
2. Steger M, Tonelli F, Ito G, et al. Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife 2016;5:e12813.
3. Reynolds A, Doggett EA, Riddle SM, Lebakken CS, Nichols RJ. LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status. Front Mol Neurosci 2014;7:54.
4. Sheng Z, Zhang S, Bustos D, et al. Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations. Sci Transl Med 2012;4:164ra161.
5. Liu Z, Mobley JA, DeLucas LJ, Kahn RA, West AB. LRRK2 autophosphorylation enhances its GTPase activity. FASEB J 2016;30:336-347.