The Rab6-regulated KIF1C kinesin motor domain contributes to Golgi organization
Most kinesins transport cargoes bound to their C-termini and use N-terminal motor domains to move along microtubules. We report here a novel function for KIF1C: it transports Rab6A-vesicles and can influence Golgi complex organization. These activities correlate with KIF1C's capacity to bind the Gol...
I tiakina i:
| Ngā kaituhi matua: | , , |
|---|---|
| Hōputu: | Artigo |
| Reo: | Inglês |
| I whakaputaina: |
eLife Sciences Publications Ltd
2015-03-01
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| Rangatū: | eLife |
| Ngā marau: | |
| Urunga tuihono: | https://elifesciences.org/articles/06029 |
| Ngā Tūtohu: |
Kāore He Tūtohu, Me noho koe te mea tuatahi ki te tūtohu i tēnei pūkete!
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