{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Although none of the provided abstracts address CEP43 directly, several studies of related centrosomal proteins shed light on the types of functions that a centrosomal factor like CEP43 is likely to perform. Several reports describe how centrosome‐associated proteins—including those that form complexes with FOP (also known as FGFR1OP), CEP19, and CAP350—are essential for anchoring microtubules, organizing the pericentriolar material, and mediating the docking and entry of proteins into primary cilia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In these studies the centrosomal proteins not only ensure proper microtubule anchoring and organization, but also contribute to ciliary assembly and the regulated trafficking of intraflagellar transport (IFT) complexes. Disruption of these processes has been linked to defects in cell polarity, aberrant signal transduction, and oncogenic transformation. For instance, misregulation of centrosomal components is implicated in altered cell cycle progression and faulty ciliogenesis, phenomena that may underpin developmental disorders and tumor growth."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n By analogy, CEP43—a centrosomal protein of similar organizational context—can be hypothesized to contribute to the maintenance of centrosome integrity. CEP43 may be important for anchoring microtubules at the centrosome and for coordinating the interactions between centriolar satellites and the microtubule network, thereby supporting key cellular processes such as proper mitotic progression, ciliogenesis, and intracellular signaling. In this regard, CEP43 likely functions as one of the essential “building‐blocks” that ensures accurate assembly of centrosomal structures and the dynamic regulation of microtubule-dependent trafficking pathways. In disease contexts, dysregulation of centrosomal proteins with functions analogous to those described here has been associated with a range of pathologies including cancer and developmental ciliopathies.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xiumin Yan, Robert Habedanck, Erich A Nigg "}, {"type": "b", "children": [{"type": "t", "text": "A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e05-08-0810"}], "href": "https://doi.org/10.1091/mbc.e05-08-0810"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16314388"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16314388"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tomoharu Kanie, Keene Louis Abbott, Nancie Ann Mooney, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Dev Cell (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.devcel.2017.05.016"}], "href": "https://doi.org/10.1016/j.devcel.2017.05.016"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28625565"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28625565"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Yuya Nishijima, Yohei Hagiya, Tomohiro Kubo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.E17-01-0017"}], "href": "https://doi.org/10.1091/mbc.E17-01-0017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28428259"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28428259"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Joanna Y Lee, Tim Stearns "}, {"type": "b", "children": [{"type": "t", "text": "FOP is a centriolar satellite protein involved in ciliogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0058589"}], "href": "https://doi.org/10.1371/journal.pone.0058589"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23554904"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23554904"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Aleksandra Mikolajka, Xiumin Yan, Grzegorz M Popowicz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2006.03.070"}], "href": "https://doi.org/10.1016/j.jmb.2006.03.070"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16690081"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16690081"}]}]}]}