Mutations in PINK1 and parkin lead to autosomal recessive forms of familial Parkinson’s disease (PD). Studies in Drosophila first showed that PINK1 and parkin function in the same pathway, with PINK1 positively regulating parkin to control mitochondrial integrity and quality control. Mitochondrial morphology is maintained by a dynamic balance of mitochondrial fusion and fission. Mitofusin (Mfn) is a GTPase located on the mitochondrial outer membrane and controls mitochondrial fusion. Importantly, downregulation of Mfn suppresses the mutant phenotypes in PINK1 and parkin mutants. Parkin, an E3 ubiquitin ligase, degrades Mfn. Mul1 is another E3 ligase that functions in parallel to Parkin to degrades Mfn. parkin mul1 double mutants have more severe mitochondrial phenotypes and much increased Mfn levels than those flies lacking either parkin or mul1 alone. p97/cdc48/Valosin-containing protein (VCP) encodes a highly conserved and abundant AAA+ ATPase which participates in multiple cellular processes. We have found that overexpression of VCP results in a dramatic rescue of defects of mitochondrial integrity, cell death and tissue damage due to lack of PINK1 and parkin. VCP overexpression significantly decreases Mfn levels in wildtype flies. Overexpression of VCP also decreases the accumulated Mfn levels in PINK1 or parkin null mutants. In addition, VCP overexpression suppresses the mitochondrial morphological defects in parkin mul1 double mutants. These results suggest that VCP-dependent suppression of PINK1 and parkin phenotypes occurs through downregulaton of Mfn protein level.