Journal
JOURNAL OF CELL BIOLOGY
Volume 217, Issue 2, Pages 619-633Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201708122
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- MEXT KAKENHI [JP26116007]
- Japan Society for the Promotion of Science
- Japan Society for the Promotion of Science KAKENHI [JP24770130, JP26440032, JP17K07310, JP24247038, JP25112518, JP25116717, JP15K14511, JP15K21743, JP17H03675]
- Takeda Science Foundation
- Naito Foundation
- Japan Foundation for Applied Enzymology
- Novartis Foundation (Japan) for the Promotion of Science
- Grants-in-Aid for Scientific Research [15K21743, 17K07310, 26116007, 17H03675] Funding Source: KAKEN
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Microtubule-dependent long-distance movement of peroxisomes occurs in mammalian cells. However, its molecular mechanisms remain undefined. In this study, we identified three distinct splicing variants of human mitochondrial Rho GTPase-1 (Miro1), each containing amino acid sequence insertions 1 (named Miro1-var2), 2 (Miro1-var3), and both 1 and 2 (Miro1-var4), respectively, at upstream of the transmembrane domain. Miro1-var4 and Miro1-var2 are localized to peroxisomes in a manner dependent on the insertion 1 that is recognized by the cytosolic receptor Pex19p. Exogenous expression of Miro1-var4 induces accumulation of peroxisomes at the cell periphery and augments long-range movement of peroxisomes along microtubules. Depletion of all Miro1 variants by knocking down MIRO1 suppresses the long-distance movement of peroxisomes. Such abrogated movement is restored by reexpression of peroxisomal Miro1 variants. Collectively, our findings identify for the first time peroxisome-localized Miro1 variants as adapter proteins that link peroxisomes to the microtubule-dependent transport complexes including TRAK2 in the intracellular translocation of peroxisomes in mammalian cells.
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