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A VDAC1-Derived N-Terminal Peptide Inhibits Mutant SOD1-VDAC1 Interactions and Toxicity in the SOD1 Model of ALS

Shteinfer-Kuzmine, Anna (author)
Ben Gurion Univ Negev, Dept Life Sci, Natl Inst Biotechnol Negev, Beer Sheva, Israel
Argueti, Shirel (author)
Ben Gurion Univ Negev, Dept Physiol & Cell Biol, Fac Hlth Sci, Zlotowski Ctr Neurosci, Beer Sheva, Israel
Gupta, Rajeev (author)
Ben Gurion Univ Negev, Dept Life Sci, Natl Inst Biotechnol Negev, Beer Sheva, Israel
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Shvil, Neta (author)
Ben Gurion Univ Negev, Dept Physiol & Cell Biol, Fac Hlth Sci, Zlotowski Ctr Neurosci, Beer Sheva, Israel
Abu-Hamad, Salah (author)
Ben Gurion Univ Negev, Dept Physiol & Cell Biol, Fac Hlth Sci, Zlotowski Ctr Neurosci, Beer Sheva, Israel
Gropper, Yael (author)
Ben Gurion Univ Negev, Dept Physiol & Cell Biol, Fac Hlth Sci, Zlotowski Ctr Neurosci, Beer Sheva, Israel
Hoeber, Jan, 1986- (author)
Uppsala universitet,Institutionen för neurovetenskap
Magri, Andrea (author)
Univ Catania, Dept Biol Geol & Environm Sci, Catania, Italy
Messina, Angela (author)
Univ Catania, Dept Biol Geol & Environm Sci, Catania, Italy
Kozlova, Elena N. (author)
Uppsala universitet,Institutionen för neurovetenskap
Shoshan-Barmatz, Varda (author)
Ben Gurion Univ Negev, Dept Life Sci, Natl Inst Biotechnol Negev, Beer Sheva, Israel
Israelson, Adrian (author)
Ben Gurion Univ Negev, Dept Physiol & Cell Biol, Fac Hlth Sci, Zlotowski Ctr Neurosci, Beer Sheva, Israel
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 (creator_code:org_t)
2019-08-14
2019
English.
In: Frontiers in Cellular Neuroscience. - : FRONTIERS MEDIA SA. - 1662-5102. ; 13
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Mutations in superoxide dismutase (SOD1) are the second most common cause of familial amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease caused by the death of motor neurons in the brain and spinal cord. SOD1 neurotoxicity has been attributed to aberrant accumulation of misfolded SOD1, which in its soluble form binds to intracellular organelles, such as mitochondria and ER, disrupting their functions. Here, we demonstrate that mutant SOD1 binds specifically to the N-terminal domain of the voltage-dependent anion channel (VDAC1), an outer mitochondrial membrane protein controlling cell energy, metabolic and survival pathways. Mutant SOD1(G93A) and SOD1(G85R), but not wild type SOD1, directly interact with VDAC1 and reduce its channel conductance. No such interaction with N-terminal-truncated VDAC1 occurs. Moreover, a VDAC1-derived N-terminal peptide inhibited mutant SOD1-induced toxicity. Incubation of motor neuron-like NSC-34 cells expressing mutant SOD1 or mouse embryonic stem cell-derived motor neurons with different VDAC1 N-terminal peptides resulted in enhanced cell survival. Taken together, our results establish a direct link between mutant SOD1 toxicity and the VDAC1 N-terminal domain and suggest that VDAC1 N-terminal peptides targeting mutant SOD1 provide potential new therapeutic strategies for ALS.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

ALS
misfolded SOD1
mutant SOD1
N-terminal peptide
VDAC1

Publication and Content Type

ref (subject category)
art (subject category)

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