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In a new study, Mark Cookson of the National Institute on Aging and colleagues found that a common genetic mutation associated with Parkinson's disease drives iron mislocalization in activated microglia
.
The results may help explain the accumulation of toxic iron in affected brain regions in this disease and provide a basis for the development of therapies aimed at correcting this iron transport defect
Mutations in the LRRK2 gene are responsible for approximately 5% of familial Parkinson's disease cases and 1% of non-familial Parkinson's disease cases
.
LRRK2 is a kinase that regulates other proteins by adding phosphate groups, and pathogenic mutations are known to increase the kinase activity of this enzyme
To understand how the LRRK2 mutation found in Parkinson's disease might affect this process, the authors first visualized Rab8a movement in mouse astrocytes with pathogenic mutations in LRRK2
.
They found that this mutant LRRK2 is responsible for redirecting Rab8a from its normal location in the endocytic recycling compartment and sequestering it in damaged lysosomes
G2019S-mutated LRRK2 induces iron accumulation in inflammatory microglia in vivo
.
Image via PLoS Biology, 2021, doi:10.
This mislocalization of Rab8a has a distinct effect on transferrin receptors: in cells containing normal LRRK2, transferrin receptors are distributed across multiple vesicle types
.
However, in cells harboring Parkinson's disease-mutated LRRK2, the transferrin receptor and its iron instead accumulate in damaged lysosomes in the presence of Rab8a and mutated LRRK2
Note: The original text has been deleted
References:
Adamantios Mamais et al.
