دورية أكاديمية

The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to alpha-tubulin1: Possible implications for cilia-specific tubulin entry

التفاصيل البيبلوغرافية
العنوان: The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to alpha-tubulin1: Possible implications for cilia-specific tubulin entry
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
الوصف
تدمد:13989219
16000854
DOI:10.1111/tra.12461