Mukherjee, Joyita ; Mahato, Biraj ; Adhya, Samit (2014) Vesicular transport of a ribonucleoprotein to mitochondria Biology Open, 3 (11). pp. 1083-1091. ISSN 2046-6390
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Official URL: http://doi.org/10.1242/bio.20149076
Related URL: http://dx.doi.org/10.1242/bio.20149076
Abstract
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to The Company of Biologists Ltd. |
Keywords: | RNA protein complex, Endosome, Sorting, Caveolin 1, Mitochondria |
ID Code: | 129190 |
Deposited On: | 22 Nov 2022 10:50 |
Last Modified: | 22 Nov 2022 10:50 |
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