DOI: 10.1083/jcb.200507087. Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network

Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network

10.1083/jcb.200507087

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

Mutations in GDAP1 lead to severe forms of the peripheral motor and sensory neuropathy, Charcot-Marie-Tooth disease (CMT), which is characterized by heterogeneous phenotypes, including pronounced axonal damage and demyelination. We show that neurons and Schwann cells express ganglioside-induced differentiation associated protein 1 (GDAP1), which suggest that both cell types may contribute to the mixed features of the disease. GDAP1 is located in the mitochondrial outer membrane and regulates the mitochondrial network. Overexpression of GDAP1 induces fragmentation of mitochondria without inducing apoptosis, affecting overall mitochondrial activity, or interfering with mitochondrial fusion. The mitochondrial fusion proteins, mitofusin 1 and 2 and Drp1(K38A), can counterbalance the GDAP1-dependent fission. GDAP1-specific knockdown by RNA interference results in a tubular mitochondrial morphology. GDAP1 truncations that are found in patients who have CMT are not targeted to mitochondria and have lost mitochondrial fragmentation activity. The latter activity also is reduced strongly for disease-associated GDAP1 point mutations. Our data indicate that an exquisitely tight control of mitochondrial dynamics, regulated by GDAP1, is crucial for the proper function of myelinated peripheral nerves.

Bibliography

Niemann, A., Ruegg, M., La Padula, V., Schenone, A., & Suter, U. (2005). Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network. The Journal of Cell Biology, 170(7), 1067â1078.

Authors 5

Axel Niemann (first)
Marcel Ruegg (additional)
Veronica La Padula (additional)
Angelo Schenone (additional)
Ueli Suter (additional)

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Dates

Type	When
Created	19 years, 11 months ago (Sept. 19, 2005, 8:25 p.m.)
Deposited	1 year, 6 months ago (Jan. 29, 2024, 8:46 p.m.)
Indexed	2 days, 2 hours ago (Aug. 23, 2025, 9:39 p.m.)
Issued	19 years, 11 months ago (Sept. 19, 2005)
Published	19 years, 11 months ago (Sept. 19, 2005)
Published Online	19 years, 11 months ago (Sept. 19, 2005)
Published Print	19 years, 10 months ago (Sept. 26, 2005)

Funders 0

None

BibTeX

@article{Niemann_2005, title={Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network}, volume={170}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200507087}, DOI={10.1083/jcb.200507087}, number={7}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Niemann, Axel and Ruegg, Marcel and La Padula, Veronica and Schenone, Angelo and Suter, Ueli}, year={2005}, month=sep, pages={1067–1078} }

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  "abstract": "<jats:p>Mutations in GDAP1 lead to severe forms of the peripheral motor and sensory neuropathy, Charcot-Marie-Tooth disease (CMT), which is characterized by heterogeneous phenotypes, including pronounced axonal damage and demyelination. We show that neurons and Schwann cells express ganglioside-induced differentiation associated protein 1 (GDAP1), which suggest that both cell types may contribute to the mixed features of the disease. GDAP1 is located in the mitochondrial outer membrane and regulates the mitochondrial network. Overexpression of GDAP1 induces fragmentation of mitochondria without inducing apoptosis, affecting overall mitochondrial activity, or interfering with mitochondrial fusion. The mitochondrial fusion proteins, mitofusin 1 and 2 and Drp1(K38A), can counterbalance the GDAP1-dependent fission. GDAP1-specific knockdown by RNA interference results in a tubular mitochondrial morphology. GDAP1 truncations that are found in patients who have CMT are not targeted to mitochondria and have lost mitochondrial fragmentation activity. The latter activity also is reduced strongly for disease-associated GDAP1 point mutations. Our data indicate that an exquisitely tight control of mitochondrial dynamics, regulated by GDAP1, is crucial for the proper function of myelinated peripheral nerves.</jats:p>",
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