Engelender Simone - Associate Professor
Main Research Area
We study the molecular mechanisms involved in Parkinson’s disease. We investigate how proteins involved in the disease, in special α-synuclein and synphilin-1 isoforms, form Lewy body-like inclusions. We also investigate how their ubiquitylation contributes to the formation of inclusions. We propose that ubiquitylation of synphilin-1 and α-synuclein represents a primary event for the formation of Lewy bodies and to pathogenesis of the disease.
Items 1 – 14
1: Szargel, R., Rott, R., Eyal, A., Haskin, Y., Shani V. and Engelender, S.
Synphilin-1A inhibits SIAH and modulates a-synuclein monoubiquitylation and inclusion formation
J. Biol. Chem. 01/01/2009; 284: 11706 – 11716
2: Engelender, S.
Monoubiquitylation of a-synuclein and autophagy in Parkinson’s disease
Autophagy 01/01/2008; 4: 372 – 374
3: Rott R., Szargel R., Liani, E., Haskin, J., Shani, V., Avraham E., and Engelender S.
Monoubiquitylation of a-synuclein by SIAH promotes its aggregation in dopaminergic cells
J. Biol. Chem. 01/01/2008; 283: 3316 – 3328
4: Szargel R., Rott R. and Engelender, S.
Synphilin-1 isoforms in Parkinson’s disease: regulation by phosphorylation and ubiquitylation
Cell Mol Life Sci 01/01/2008; 65: 80 – 88
5: Avraham E., Rott R., Liani, E., Szargel R., and Engelender S.
Phosphorylation of parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation
J. Biol. Chem. 01/01/2007; 282: 12842 – 12850
6: Eyal, A. and Engelender, S.
Synphilin isoforms and the search for a cellular model of Lewy body formation in Parkinson’s disease
Cell Cycle 01/01/2006; 5: 2082 – 2086
7: Eyal, A., Szargel, R., Avraham, E., Liani, E., Haskin, Y., Rott, R., and Engelender, S.
Synphilin-1A: A novel aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from a-synucleinopathy patients.
Proc. Natl. Acad. Sci. U.S.A. 01/01/2006; 103: 5917 – 5922
8: Avraham E, Szargel R, Eyal A, Rott R, Engelender S.
GSK3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: Implications for proteasomal function and Lewy body formation.
J. Biol. Chem. 13/09/2005; 280: 42877 – 42886
9: Liani, E., Eyal, A., Avraham, E., Shemer, R., Szargel, R., Berg, D., Bornemann, A., Riess, O., Ross, C.A., Rott, R., and Engelender, S.
Ubiquitylation of synphilin-1 and a-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson”s disease.
Proc. Natl. Acad. Sci. U.S.A. 01/04/2004; 101: 5500 – 5505
10: Ribeiro, C.S., de Paula, K.C., Ross, C.A., Menezes, J.R.J., and Engelender, S.
Synphilin-1 is developmentally localized to synaptic terminals and its association with synaptic vesicles is modulated by a-synuclein.
J. Biol. Chem. 01/06/2002; 277: 23927 – 23933
11: Tanaka, Y., Engelelnder, S., Igarashi, S., Rao, R.K., Wanner, T.,Tanzi R.E., Sawa, A., Dawson, V.L. Dawson, T.M. and Ross, C.A.
Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis.
Hum. Mol. Genet. 01/04/2001; 10: 919 – 926
12: Engelender, S., Wanner, T., Kleiderlein, J.J., Ashworth, R., Wakabayashi, K.,Tsuji, S., Takahashi, H., Margolis, R.L. and Ross, C.A.
Organization of The human synphilin-1 gene, a candidate for Parkinson’s disease.
Mamm. Genome 01/09/2000; 11: 763 – 766
13: Wakabayashi, K., Engelender, S., Yoshimoto, M., Tsuji, S., Ross, C.A. and Takahashi, H.
Synphilin-1 is present in Lewy bodies in Parkinson”s disease.
Ann. Neurol. 01/04/2000; 47: 521 – 523
14: Engelender, S., Kaminsky, Z., Guo, X., Sharp, A.H., Amaravi, R.K., Kleiderlein, J.J., Margolis, R.L., Troncoso, J.C., Lanahan, A.A., Worley, P.F., Dawson, V.L., Dawson, T.M. and Ross, C.A.
Synphilin-1: A protein that associates with alpha-synuclein and promotes the formation of cytosolic inclusions.
Nature Genet. 01/05/1999; 22: 110 – 114