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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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The Company of Biologists
2014-10-01
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| Series: | Biology Open |
| Subjects: | |
| Online Access: | http://bio.biologists.org/content/3/11/1083 |
| _version_ | 1818461252377116672 |
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| author | Joyita Mukherjee Biraj Mahato Samit Adhya |
| author_facet | Joyita Mukherjee Biraj Mahato Samit Adhya |
| author_sort | Joyita Mukherjee |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T23:43:11Z |
| format | Article |
| id | doaj.art-c3700e25868f491aa08c756bbec26773 |
| institution | Directory Open Access Journal |
| issn | 2046-6390 |
| language | English |
| last_indexed | 2024-12-14T23:43:11Z |
| publishDate | 2014-10-01 |
| publisher | The Company of Biologists |
| record_format | Article |
| series | Biology Open |
| spelling | doaj.art-c3700e25868f491aa08c756bbec267732022-12-21T22:43:28ZengThe Company of BiologistsBiology Open2046-63902014-10-013111083109110.1242/bio.2014907620149076Vesicular transport of a ribonucleoprotein to mitochondriaJoyita MukherjeeBiraj Mahato0Samit Adhya Present address: Penn Institute for Regenerative Medicine, University of Pennsylvania, 3800 Spruce Street, Philadelphia, PA 19104, USA. 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.http://bio.biologists.org/content/3/11/1083RNA protein complexEndosomeSortingCaveolin 1Mitochondria |
| spellingShingle | Joyita Mukherjee Biraj Mahato Samit Adhya Vesicular transport of a ribonucleoprotein to mitochondria Biology Open RNA protein complex Endosome Sorting Caveolin 1 Mitochondria |
| title | 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_short | Vesicular transport of a ribonucleoprotein to mitochondria |
| title_sort | vesicular transport of a ribonucleoprotein to mitochondria |
| topic | RNA protein complex Endosome Sorting Caveolin 1 Mitochondria |
| url | http://bio.biologists.org/content/3/11/1083 |
| work_keys_str_mv | AT joyitamukherjee vesiculartransportofaribonucleoproteintomitochondria AT birajmahato vesiculartransportofaribonucleoproteintomitochondria AT samitadhya vesiculartransportofaribonucleoproteintomitochondria |