Selected Publications
- Fogel A.I., Dlouhy, B.J., Wang, C., Ryu, S.W., Neutzner, A., Hasson, S.A., Sideris, D.P., Abeliovich, H., and R.J. Youle (2013). Role of membrane association and Atg14-dependent phosphorylation in beclin-1 mediated autophagy. Molecular and Cellular Biology 33(18): 3675-3688.
- Abeliovich, H. Zarei, M., Rigbolt, K., Youle, R. and Dengjel, J. (2013). Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy. Nature Communications 4:2789.
- Ecker, N., Mor, A., Journo, D., and H. Abeliovich (2010). Induction of autophagic flux by amino acid deprivation is distinct from nitrogen starvation-induced macroautophagy. Autophagy 6: 879-890.
- Journo, D., Mor A., and H. Abeliovich (2009). Aup1 mediated regulation of Rtg3 during mitophagy. J. Biol Chem. 284(51):35885-35895.
- Tal, R., Winter, G., Ecker, N., Klionsky, D.J., and H. Abeliovich (2007). Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J. Biol. Chem. 282:5617-5624.
FRIAS Project
Mechanisms of intra-mitochondrial selectivity during mitophagy
Mitophagy, or the autophagic degradation of mitochondria, is an important housekeeping function of eukaryotic cells. Mitophagy is thought to delay aging, and defects in mitophagy have been linked to disorders such as Parkinson’s disease and type II diabetes. Our preliminary data suggests that fission and fusion of mitochondria is linked to the segregation of defective mitochondrial compartments from undamaged ones, in a ‘distillation’ mechanism that leads to the selective turnover of defective compartments. Previously, we carried out a proteomic screen that identified mitochondrial matrix proteins that were selectively accumulated in mitophagy mutants relative to wild?type cells under mitophagic conditions. We showed that these proteins are indeed mitophagocytosed at higher rates, relative to other matrix proteins and are segregated from proteins that show low rates of mitophagy. Our central hypothesis is that active intra?mitochondrial protein sorting underlies the segregation of defective mitochondrial sub?compartments, and that specific proteins and gene products are required for this sorting to occur. Our specific aims are: 1) To identify mitochondrial matrix proteins that depend on Dnm1 for their mitophagic degradation. 2) To measure and compare the mobility of proteins that depend on Dnm1 for degradation, with that of proteins whose degradation is Dnm1? independent. 3) To visualize intra?matrix sub domains by immuno?EM analysis of segregated mitochondrial proteins.