Mutations in PTEN-induced Kinase 1 (PINK1) and parkin lead to autosomal recessive forms of Parkinson’s disease (PD). PINK1 encodes a putative Ser/Thr kinase with a mitochondrial targeting sequence, and parkin encodes an E3 ubiquitin ligase. We and others have previously shown that PINK1 and parkin function in the same genetic pathway to regulate mitochondrial integrity and quality in Drosophila. PINK1/parkin null mutant flies show motility defects and apoptotic muscle death, and mitochondria in neurons and muscles exhibit abnormal morphology and compromised function. Loss of PINK1 in human cells block Parkin-mediated autophagy of damaged mitochondria (mitophagy), an important mechanism of mitochondrial quality control. Here we identified a new familiar form of PINK1 mutation in a PD patient family. We found that two PD patients in this family carried two different PINK1 mutant alleles: one was a previously characterized PINK1 L347P allele; the other was an uncharacterized splicing mutant resulting in skipping of PINK1 Exon7. As PINK1 Exon7 encodes the C-terminus of the kinase domain, we investigated whether ΔExon7 PINK1 is a loss-of-function allele. We showed that overexpression of human ΔExon7 PINK1 failed to rescue mitophagy defects in PINK1 knockout HeLa cells, in contrast to the human wildtype PINK1; overexpression of the Drosophila homolog of ΔExon7 PINK1 also failed to rescue mitochondrial morphology defects and apoptotic muscle death in PINK1 null mutant flies, in contrast to the wildtype Drosophila PINK1. In this study, we validated two model systems (Drosophila muscle in vivo and human cell-based mitophagy assay) for future characterization of newly discovered PD-linked mutations.