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You are here: FRIAS Fellows Fellows 2017/18 Prof. Dr. Hagai Abeliovich

Prof. Dr. Hagai Abeliovich

The Hebrew University of Jerusalem
Cell Biology
External Senior Fellow (Marie S. Curie FCFP)
July - September 2016


1984-1987: B.Sc. in Chemistry and Biology, Hebrew University of Jerusalem, Cum Laude; 1988-1990: M.Sc. in Biochemistry, Hebrew University of Jerusalem, Cum Laude; 1991-1996: Ph.D. in Molecular Biology, at the Institute of  Microbiology,  Hadassa Medical School, Hebrew University of Jerusalem; 1997: Postdoctoral fellow, Dept. of Cell Biology, Yale University School of Medicine, in the lab of Dr. Susan Ferro-Novick; 1998-2002: Postdoctoral fellow, mentored (jointly) in the labs of Drs. Scott Emr (UCSD) and Daniel Klionsky (UC-Davis and currently at the University of Michigan).

2002- 2004: Lecturer, Institute of Biochemistry, Food Science, and Nutrition at the Faculty of Agricultural, Food, and Environmental Quality Sciences; 2004-2013: Senior lecturer, Institute of Biochemistry and Food Science, Faculty of Agricultural, Food, and Environmental Quality Sciences (tenure granted in July 2008); 2013-present: Associate professor, Institute of Biochemistry and Food Science, Faculty of Agricultural, Food, and Environmental Quality Sciences

2010-2011: Adjunct Investigator, National Institute for Neurological Disorders and Stroke (Bethesda, MD). Sponsored by Dr. Richard Youle while on sabbatical from HU.

2007-present: Member, editorial board of “Autophagy”, a Landes Bioscience publication. 2013-present: Member of the editorial board of “The Journal of Biological Chemistry”.


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 Research 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.