Identification of potential protein interactors of Lrrk2.
Pathogenic substitutions in the Lrrk2 protein have been shown to be an important cause of both familial and sporadic parkinsonism. The molecular pathway involved in Lrrk2 dopaminergic neuron degeneration remains elusive. Employing a combination of Lrrk2-mediated protein precipitation and tandem mass spectrometry, we identified 14 potential Lrrk2 binding partners. The majority of these interactions may be subgrouped into three functional cellular pathways: (i) chaperone-mediated response, (ii) proteins associated with the cytoskeleton and trafficking and (iii) phosphorylation and kinase activity. Future investigation of these candidates is now warranted and may help resolve the pathomechanism behind Lrrk2 neurodegeneration.
Dächsel
Justus C
JC
Department of Neuroscience and Neurology, Mayo Clinic College of Medicine, Birdsall Building, Jacksonville, FL 32224, USA.
Taylor
Julie P
JP
Mok
Su San
SS
Ross
Owen A
OA
Hinkle
Kelly M
KM
Bailey
Rachel M
RM
Hines
Jacob H
JH
Szutu
Jennifer
J
Madden
Benjamin
B
Petrucelli
Leonard
L
Farrer
Matthew J
MJ
D002461:Cell Line, Transformed; D006801:Humans; D047468:Immunoprecipitation / Q000379:methods; D000071158:Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; D013058:Mass Spectrometry / Q000379:methods; D008970:Molecular Weight; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism
D011506:Proteins; C495280:LRRK2 protein, human; D000071158:Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; D017346:Protein Serine-Threonine Kinases