The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
2006 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 344, no 2, 500-510 p.Article in journal (Refereed) Published
We recently described the atypical Rho GTPases Miro-1 and Miro-2. These proteins have tandem GTP-binding domains separated by a linker region with putative calcium-binding motives. In addition, the Miro GTPases have a C-terminal transmembrane domain, which confers targeting to the mitochondria. It was reported previously that a constitutively active mutant of Miro-1 induced a clustering of the mitochondria. This response can be separated into two distinct phenotypes: a formation of aggregated mitochondria and the appearance of thread-like mitochondria probably caused by defects in mitochondrial trafficking. The first GTPase domain is required for the clustering of the mitochondria, but the effect is not dependent on the EF-hands. Miro-2 only induces aggregation and not the formation of thread-like mitochondria. Moreover, we show that Miro interacts with the Kinesin-binding proteins, GRIF-1 and OIP106, suggesting that the Miro GTPases form a link between the mitochondria and the trafficking apparatus of the microtubules.
Place, publisher, year, edition, pages
2006. Vol. 344, no 2, 500-510 p.
Animals, COS Cells, Cell Line, Cercopithecus aethiops, Humans, Kidney/*metabolism, Mitochondria/*metabolism, Mitochondrial Proteins/genetics/*metabolism, Protein Transport/physiology, Research Support; Non-U.S. Gov't, Structure-Activity Relationship, rho GTP-Binding Proteins/genetics/*metabolism
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-96849DOI: 10.1016/j.bbrc.2006.03.163PubMedID: 16630562OAI: oai:DiVA.org:uu-96849DiVA: diva2:171564