دورية أكاديمية
The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to alpha-tubulin1: Possible implications for cilia-specific tubulin entry
العنوان: | The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to alpha-tubulin1: Possible implications for cilia-specific tubulin entry |
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المؤلفون: | GIROTRA, M, SRIVASTAVA, S, KULKARNI, A, BARBORA, A, BOBRA, K, GHOSAL, D, DEVAN, P, AHER, A, JAIN, A, PANDA, D, RAY, K |
بيانات النشر: | WILEY-BLACKWELL |
سنة النشر: | 2017 |
مصطلحات موضوعية: | Sensory Cilia, Ncd Tail, Caenorhabditis-Elegans, Chlamydomonas Flagella, Alpha-Tubulin, Transport, Microtubules, Protein, Isotypes, Complex, Antenna, Cilia, Drosophila, Kif3a, Kif3b, Kinesin-Like-Protein 64d, Kinesin-Like-Protein 68d, Mouse |
الوصف: | The assembly of microtubule-based cytoskeleton propels the cilia and flagella growth. Previous studies have indicated that the kinesin-2 family motors transport tubulin into the cilia through intraflagellar transport. Here, we report a direct interaction between the C-terminal tail fragments of heterotrimeric kinesin-2 and -tubulin1 isoforms in vitro. Blot overlay screen, affinity purification from tissue extracts, cosedimentation with subtilisin-treated microtubule and LC-ESI-MS/MS characterization of the tail-fragment-associated tubulin identified an association between the tail domains and -tubulin1A/D isotype. The interaction was confirmed by Forster's resonance energy transfer assay in tissue-cultured cells. The overexpression of the recombinant tails in NIH3T3 cells affected the primary cilia growth, which was rescued by coexpression of a -tubulin1 transgene. Furthermore, fluorescent recovery after photobleach analysis in the olfactory cilia of Drosophila indicated that tubulin is transported in a non-particulate form requiring kinesin-2. These results provide additional new insight into the mechanisms underlying selective tubulin isoform enrichment in the cilia. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
تدمد: | 1398-9219 1600-0854 |
العلاقة: | TRAFFIC,18(2)123-133; http://dx.doi.org/10.1111/tra.12461Test |
DOI: | 10.1111/tra.12461 |
الإتاحة: | https://doi.org/10.1111/tra.12461Test |
رقم الانضمام: | edsbas.763E9DCB |
قاعدة البيانات: | BASE |
تدمد: | 13989219 16000854 |
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DOI: | 10.1111/tra.12461 |