The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells | Zendy

Daniel Tondera | Zendy; Frank Czauderna | Zendy; Katharina Paulick | Zendy; Rolf Schwarzer | Zendy; Jörg Kaufmann | Zendy; Ansgar Santel | Zendy

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The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells

Author(s) -

Daniel Tondera,

Frank Czauderna,

Katharina Paulick,

Rolf Schwarzer,

Jörg Kaufmann,

Ansgar Santel

Publication year - 2005

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.02415

Subject(s) - mitochondrial fission , biology , dnaja3 , mitochondrial fusion , microbiology and biotechnology , mitochondrial apoptosis induced channel , mitochondrion , atp–adp translocase , mitochondrial carrier , rna interference , translocase of the inner membrane , hspa9 , fission , inner mitochondrial membrane , mitochondrial membrane transport protein , mfn1 , mitochondrial dna , rna , bacterial outer membrane , biochemistry , gene , peptide sequence , physics , quantum mechanics , neutron , escherichia coli

Mitochondria are dynamic organelles that change morphology by controlled fission and fusion events. Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mitochondrial fission. Upon overexpression of MTP18, mitochondrial morphology was altered from filamentous to punctate structures suggesting excessive mitochondrial fission. Mitochondrial fragmentation was blocked in cells coexpressing either the mitochondrial fusion protein Mfn1 or Drp1(K38A), a dominant negative version of the fission protein Drp1. Also, a loss-of function of endogenous MTP18 by RNA interference (RNAi) resulted in highly fused mitochondria. Moreover, MTP18 appears to be required for mitochondrial fission because it is blocked after overexpression of hFis1 in cells with RNAi-mediated MTP18 knockdown. In conclusion, we propose that MTP18 functions as an essential intramitochondrial component of the mitochondrial division apparatus, contributing to the maintenance of mitochondrial morphology.

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