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Characterizing the Roles of PF16 and FAP81 in the Regulation of Flagellar Motility
Başlık:
Characterizing the Roles of PF16 and FAP81 in the Regulation of Flagellar Motility
Yazar:
Loreng, Thomas Daniel, author.
ISBN:
9780438009677
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (188 pages)
Genel Not:
Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
Includes supplementary digital materials.
Advisors: Elizabeth F. Smith Committee members: Yina H. Huang; James B. Moseley; Winfield S. Sale; Roger D. Sloboda.
Özet:
Cilia and flagella are complex microtubule-based organelles that are remarkably well-conserved throughout evolution. Motile cilia are composed of a microtubule skeleton consisting of a classically defined "9+2" structure known as the axoneme. Using force generated by dynein motors on the outer nine doublet microtubules, motile cilia produce intricate beating waveforms. In the center of the axoneme are two single microtubules, termed C1 and C2, and their associated protein projections; collectively known as the central apparatus. The central apparatus projections consist of interconnected proteins and protein complexes that are strongly implicated in the regulation of axonemal dynein. One such protein is PF16, which, when missing from the axoneme, causes flagellar paralysis and the instability of the C1 microtubule. The objective of the research presented in this dissertation was to examine the mechanism by which PF16 regulates ciliary motility and to identify PF16-interacting proteins in the axoneme. Using Chlamydomonas strains containing epitope-tagged PF16, I observed a phenotype where cells were unable to switch from an asymmetric to a symmetric waveform. Coupled with our previous collaborative work in localizing PF16 using cryo-electron tomography, these findings suggest that PF16 is involved in regulating waveform switching via contacts with the radial spoke heads. To dissect the mechanism by which PF16 regulates motility, attempts were made to identify PF16-interacting proteins. In mammals, the homolog of PF16 is said to interact with other known central apparatus proteins: PF6 and PF20. Using biochemical and chromatographic techniques, I found no evidence for these findings. Furthermore, previous characterization of PF6 in Chlamydomonas showed no such interaction. To determine true axonemal interactors, a quantitative mass spectrometry approach was taken. Using this approach, I was able to identify FAP81 as a potential C1-associated and PF16-interacting protein. In addition, I was able to show that FAP81 is necessary for proper ciliary motility. Combined, my results point to the importance of PF16 and the central apparatus in regulating waveform switching while also pointing toward a previously uncharacterized PF16-containing complex. Future challenges include determining the precise molecular mechanism by which PF16 and FAP81 regulate ciliary motility and confirming a direct protein-protein interaction between them.
Notlar:
School code: 0059
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(681880.1) | 681880-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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