dc.contributor.author | Antoniades, Ioanna | en |
dc.contributor.author | Stylianou, Panayiota | en |
dc.contributor.author | Christodoulou, Neophytos | en |
dc.contributor.author | Skourides, Paris A. | en |
dc.creator | Antoniades, Ioanna | en |
dc.creator | Stylianou, Panayiota | en |
dc.creator | Christodoulou, Neophytos | en |
dc.creator | Skourides, Paris A. | en |
dc.date.accessioned | 2019-11-04T12:50:11Z | |
dc.date.available | 2019-11-04T12:50:11Z | |
dc.date.issued | 2017 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/52923 | |
dc.description.abstract | We previously identified focal adhesion kinase (FAK) as an important regulator of ciliogenesis in multiciliated cells. FAK and other focal adhesion (FA) proteins associate with the basal bodies and their striated rootlets and form complexes named ciliary adhesions (CAs). CAs display similarities with FAs but are established in an integrin independent fashion and are responsible for anchoring basal bodies to the actin cytoskeleton during ciliogenesis as well as in mature multiciliated cells. FAK down-regulation leads to aberrant ciliogenesis due to impaired association between the basal bodies and the actin cytoskeleton, suggesting that FAK is an important regulator of the CA complex. However, the mechanism through which FAK functions in the complex is not clear, and in this study we examined the role of this protein in both ciliogenesis and ciliary function.Weshow that localization of FAK at CAs depends on interactions taking place at the amino-terminal (FERM) and carboxyl-terminal (FAT) domains and that both domains are required for proper ciliogenesis and ciliary function. Furthermore, we show that an interaction with another CA protein, paxillin, is essential for correct localization of FAK in multiciliated cells. This interaction is indispensable for both ciliogenesis and ciliary function. Finally, we provide evidence that despite the fact that FAK is in the active, open conformation at CAs, its kinase activity is dispensable for ciliogenesis and ciliary function revealing that FAK plays a scaffolding role in multiciliated cells. Overall these data show that the role of FAK at CAs displays similarities but also important differences compared with its role at FAs. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc. | en |
dc.source | Journal of Biological Chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85009752543&doi=10.1074%2fjbc.M116.767111&partnerID=40&md5=9aaf80541e5238bf1cdb417b3fe156d9 | |
dc.subject | adult | en |
dc.subject | controlled study | en |
dc.subject | female | en |
dc.subject | immunohistochemistry | en |
dc.subject | protein expression | en |
dc.subject | down regulation | en |
dc.subject | nonhuman | en |
dc.subject | Article | en |
dc.subject | metabolism | en |
dc.subject | phenotype | en |
dc.subject | Animals | en |
dc.subject | animal | en |
dc.subject | animal cell | en |
dc.subject | animal experiment | en |
dc.subject | genetics | en |
dc.subject | protein function | en |
dc.subject | DNA sequence | en |
dc.subject | protein interaction | en |
dc.subject | protein localization | en |
dc.subject | enzymology | en |
dc.subject | Cells | en |
dc.subject | Cytology | en |
dc.subject | Cilia | en |
dc.subject | Actin cytoskeleton | en |
dc.subject | cellular parameters | en |
dc.subject | Adhesion | en |
dc.subject | carboxy terminal sequence | en |
dc.subject | embryo | en |
dc.subject | protein domain | en |
dc.subject | Xenopus protein | en |
dc.subject | Xenopus Proteins | en |
dc.subject | actin filament | en |
dc.subject | amino terminal sequence | en |
dc.subject | avian protein | en |
dc.subject | Avian Proteins | en |
dc.subject | Basal Bodies | en |
dc.subject | bioassay | en |
dc.subject | Carboxyl-terminal | en |
dc.subject | cell adhesion | en |
dc.subject | cell culture | en |
dc.subject | chicken | en |
dc.subject | Chickens | en |
dc.subject | Ciliary functions | en |
dc.subject | ciliary motility | en |
dc.subject | ciliogenesis | en |
dc.subject | cilium | en |
dc.subject | Down-regulation | en |
dc.subject | enzyme mechanism | en |
dc.subject | Enzymes | en |
dc.subject | eukaryotic flagellum | en |
dc.subject | Focal adhesion kinase | en |
dc.subject | Focal Adhesion Protein-Tyrosine Kinases | en |
dc.subject | Focal adhesions | en |
dc.subject | genetic transfection | en |
dc.subject | immunoprecipitation | en |
dc.subject | Kinase activity | en |
dc.subject | kinetosome | en |
dc.subject | luteinizing hormone receptor | en |
dc.subject | microinjection | en |
dc.subject | Open conformation | en |
dc.subject | paxillin | en |
dc.subject | paxillin protein, Xenopus | en |
dc.subject | Protein Domains | en |
dc.subject | protein hydrolysate | en |
dc.subject | protein protein interaction | en |
dc.subject | Proteins | en |
dc.subject | scaffold protein | en |
dc.subject | Scaffolds (biology) | en |
dc.subject | Western blotting | en |
dc.subject | Xenopus laevis | en |
dc.title | Addressing the Functional Determinants of FAK during Ciliogenesis in Multiciliated Cells | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1074/jbc.M116.767111 | |
dc.description.volume | 292 | |
dc.description.startingpage | 488 | |
dc.description.endingpage | 504 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Βιολογικών Επιστημών / Department of Biological Sciences | |
dc.type.uhtype | Article | en |
dc.source.abbreviation | J.Biol.Chem. | en |
dc.contributor.orcid | Skourides, Paris A. [0000-0003-3502-5729] | |
dc.gnosis.orcid | 0000-0003-3502-5729 | |