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F3‐02‐01: Structure and function of alpha‐synuclein
Author(s) -
Eliezer David
Publication year - 2009
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2009.05.415
Subject(s) - alpha synuclein , biophysics , chemistry , helix (gastropod) , alpha helix , lewy body , linker , fibril , protein secondary structure , in vitro , in vivo , amyloid (mycology) , crystallography , protein structure , stereochemistry , biochemistry , biology , medicine , pathology , genetics , parkinson's disease , inorganic chemistry , ecology , disease , snail , computer science , operating system
lated to neurodegenerative diseases such as Alzheimer’s disease, Huntington’s disease, Amyotrophic lateral sclerosis, and PD. Methods: a-SN cDNA was transfected into SH-SY5Y human neuroblastoma. Translocation of a-SN was monitored by confocal laser scanning microscopy & Western blotting. Results: In autophagic condition, we identified that cytoplasmic a-SN is translocated into the nucleus of neuronal cells. Here we show that direct interaction of a-SN with nuclear cargo protein karyopherin alpha6 (KPNA) is the mechanism of nuclear translocation of a-SN and the sumoylation regulates its translocation. Nuclear translocated a-SN enhanced DNA repair through the binding with PCNA for neuronal survival. Conclusions: 1. In autophagic condition, a-SN is translocated into the nucleus. 2. Sumoylation regulates the nuclear translocation of a-SN. 3. Nuclear a-SN is involved in DNA-repair.