Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Catherine A. Perrone"'
Autor:
Eileen T. O'Toole, Catherine A. Perrone, Daniela Nicastro, Kristyn VanderWaal Mills, Raqual Bower, Katherine Augspurger, Mary E. Porter, Erin E. Dymek, Jianfeng Lin, Gang Fu, Thuc Vy Le, Elizabeth F. Smith, Douglas Tritschler
Publikováno v:
Molecular Biology of the Cell
Ciliary motility depends on both the precise spatial organization of multiple dynein motors within the 96 nm axonemal repeat, and highly coordinated interactions between different dyneins and regulatory complexes located at the base of the radial spo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b4410bf44a21d9e1139a709355fa9a6
Autor:
Alexandria Schauer, Catherine A. Perrone, Raqual Bower, Kristyn Van Der Waal Mills, Mary E. Porter, Douglas Tritschler, Jaimee Reck
Publikováno v:
Molecular Biology of the Cell
D1bLIC is a subunit of the retrograde IFT motor. Knockdown or knockout of D1bLIC has dose-dependent effects on flagellar assembly, length, motility, and signaling. iTRAQ-based proteomics identifies novel proteins altered in d1blic mutant flagella. TI
Autor:
Mary E. Porter, Winfield S. Sale, Laura A. Fox, Douglas Tritschler, Raqual Bower, Catherine A. Perrone, Joshua Mueller, Kristyn E VanderWaal
Publikováno v:
Molecular Biology of the Cell
The nexin–dynein regulatory complex (N-DRC) is implicated in the control of dynein activity as a structural component of the nexin link. This study identifies several new subunits of the N-DRC and demonstrates for the first time that it forms a dis
Autor:
Triscia W. Hendrickson, Catherine A. Perrone, Pinfen Yang, Mary E. Porter, Joshua Mueller, Kristin Wuichet, Winfield S. Sale, Paul Griffin
Publikováno v:
Molecular Biology of the Cell. 15:5431-5442
Increased phosphorylation of dynein IC IC138 correlates with decreases in flagellar microtubule sliding and phototaxis defects. To test the hypothesis that regulation of IC138 phosphorylation controls flagellar bending, we cloned the IC138 gene. IC13
Autor:
Patrick D. Taulman, Raqual Bower, Catherine A. Perrone, Bradley K. Yoder, Mary E. Porter, Douglas Tritschler
Publikováno v:
Molecular Biology of the Cell. 14:2041-2056
The assembly of cilia and flagella depends on bidirectional intraflagellar transport (IFT). Anterograde IFT is driven by kinesin II, whereas retrograde IFT requires cytoplasmic dynein 1b (cDHC1b). Little is known about how cDHC1b interacts with its c
Publikováno v:
Journal of Molecular Biology. 257:385-397
Recent structural studies indicate that a tektin heteropolymer forms a unique protofilament of flagellar microtubules. We report here the sequence of tektin C (approximately 47 kDa), predicted from its cDNA (GenBank U38523), compared to tektins A (ap
Publikováno v:
The Journal of Cell Biology
Previous studies of flagellar mutants have identified six axonemal polypeptides as components of a "dynein regulatory complex" (DRC). The DRC is though to coordinate the activity of the multiple flagellar dyneins, but its location within the axoneme
Publikováno v:
Europe PubMed Central
Tektins are a class of proteins that form filamentous polymers in the walls of ciliary and flagellar microtubules, and they may also be present in centrioles, centrosomes and mitotic spindles. We report here the cloning and sequencing of a cDNA for c
Autor:
Raqual Bower, Winfield S. Sale, Laura A. Fox, Kristyn E VanderWaal, Maureen Wirschell, Catherine A. Perrone, Eileen T. O'Toole, Ritsu Kamiya, Mary E. Porter, Joshua Mueller
To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assemble
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfc8d44644728d332570fe262d982607
https://europepmc.org/articles/PMC2704157/
https://europepmc.org/articles/PMC2704157/
Publikováno v:
Molecular biology of the cell. 16(3)
Intraflagellar transport (IFT) is a bidirectional process required for assembly and maintenance of cilia and flagella. Kinesin-2 is the anterograde IFT motor, and Dhc1b/Dhc2 drives retrograde IFT. To understand how either motor interacts with the IFT