Studies indicate that Miro may be involved in PD.

[7] In neurons, Miro interacts

with two key proteins involved in PD, PINK1 and Parkin.[6] Following depolarization
of the mitochondria, PINK1 phosphorylates Miro at multiple sites, including S156,
and Parkin ubiquitinates Miro, targeting it for proteasomal degradation.[6][7]
Degradation of Miro then halts mitochondrial transport.[6]

In mammals, RHOT2 is one of two Miro isoforms. Both isoforms share a structure
consisting of two EF-hand motifs linking two GTP-binding domains and a C-terminal
transmembrane domain that attaches the protein to the outer mitochondrial membrane
(OMM).[6][8] The EF-hand motifs serve as binding sites for the adaptor protein
Milton and the kinesin heavy chain.[9] These domains can also bind calcium ions,
and the binding results in a conformational change that dissociates the
mitochondrial surface from kinesin.[6][8]

Though the Rho GTPase family is closely associated with cancer progression, there
are few studies demonstrating such association with the atypical Miro proteins.[10]