Vesicular transport of a ribonucleoprotein to mitochondria
Intracellular trafficking of viruses and proteins commonly occurs via the early endosome in a process involving Rab5. The RNA Import Complex (RIC)-RNA complex is taken up by mammalian cells and targeted to mitochondria. Through RNA interference, it was shown that mito-targeting of the ribonucleoprot...
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The Company of Biologists
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4232766/ |
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pubmed-42327662014-11-20 Vesicular transport of a ribonucleoprotein to mitochondria Mukherjee, Joyita Mahato, Biraj Adhya, Samit Research Article Intracellular trafficking of viruses and proteins commonly occurs via the early endosome in a process involving Rab5. The RNA Import Complex (RIC)-RNA complex is taken up by mammalian cells and targeted to mitochondria. Through RNA interference, it was shown that mito-targeting of the ribonucleoprotein (RNP) was dependent on caveolin 1 (Cav1), dynamin 2, Filamin A and NSF. Although a minor fraction of the RNP was transported to endosomes in a Rab5-dependent manner, mito-targeting was independent of Rab5 or other endosomal proteins, suggesting that endosomal uptake and mito-targeting occur independently. Sequential immunoprecipitation of the cytosolic vesicles showed the sorting of the RNP away from Cav1 in a process that was independent of the endosomal effector EEA1 but sensitive to nocodazole. However, the RNP was in two types of vesicle with or without Cav1, with membrane-bound, asymmetrically orientated RIC and entrapped RNA, but no endosomal components, suggesting vesicular sorting rather than escape of free RNP from endosomes. In vitro, RNP was directly transferred from the Type 2 vesicles to mitochondria. Live-cell imaging captured spherical Cav1− RNP vesicles emerging from the fission of large Cav+ particles. Thus, RNP appears to traffic by a different route than the classical Rab5-dependent pathway of viral transport. The Company of Biologists 2014-10-17 /pmc/articles/PMC4232766/ /pubmed/25326515 http://dx.doi.org/10.1242/bio.20149076 Text en © 2014. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Mukherjee, Joyita Mahato, Biraj Adhya, Samit |
| spellingShingle |
Mukherjee, Joyita Mahato, Biraj Adhya, Samit Vesicular transport of a ribonucleoprotein to mitochondria |
| author_facet |
Mukherjee, Joyita Mahato, Biraj Adhya, Samit |
| author_sort |
Mukherjee, Joyita |
| title |
Vesicular transport of a ribonucleoprotein to mitochondria |
| title_short |
Vesicular transport of a ribonucleoprotein to mitochondria |
| title_full |
Vesicular transport of a ribonucleoprotein to mitochondria |
| title_fullStr |
Vesicular transport of a ribonucleoprotein to mitochondria |
| title_full_unstemmed |
Vesicular transport of a ribonucleoprotein to mitochondria |
| title_sort |
vesicular transport of a ribonucleoprotein to mitochondria |
| description |
Intracellular trafficking of viruses and proteins commonly occurs via the early endosome in a process involving Rab5. The RNA Import Complex (RIC)-RNA complex is taken up by mammalian cells and targeted to mitochondria. Through RNA interference, it was shown that mito-targeting of the ribonucleoprotein (RNP) was dependent on caveolin 1 (Cav1), dynamin 2, Filamin A and NSF. Although a minor fraction of the RNP was transported to endosomes in a Rab5-dependent manner, mito-targeting was independent of Rab5 or other endosomal proteins, suggesting that endosomal uptake and mito-targeting occur independently. Sequential immunoprecipitation of the cytosolic vesicles showed the sorting of the RNP away from Cav1 in a process that was independent of the endosomal effector EEA1 but sensitive to nocodazole. However, the RNP was in two types of vesicle with or without Cav1, with membrane-bound, asymmetrically orientated RIC and entrapped RNA, but no endosomal components, suggesting vesicular sorting rather than escape of free RNP from endosomes. In vitro, RNP was directly transferred from the Type 2 vesicles to mitochondria. Live-cell imaging captured spherical Cav1− RNP vesicles emerging from the fission of large Cav+ particles. Thus, RNP appears to traffic by a different route than the classical Rab5-dependent pathway of viral transport. |
| publisher |
The Company of Biologists |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4232766/ |
| _version_ |
1613156949268889600 |