Structural highlights
Publication Abstract from PubMed
Rootletin is the main component of the ciliary rootlet and functions as a centriole linker connecting the two mother centrioles. Despite the functional importance of rootletin, the molecular architecture of the rootletin filament and its assembly mechanism are poorly understood. Here, we identify the coiled-coil domain 3 (CCD3) of rootletin as the key domain for its cellular function. The crystal structure of the CCD3(1108-1317) fragment containing 28 heptad repeats and 1 hendecad repeat reveals that it forms a parallel coiled-coil dimer spanning approximately 300A in length. Crosslinking experiments and biophysical analyses of the minimal functional region of CCD3 (CCD3-6) suggest that CCD3-6 is structurally dynamic and may be important for oligomer formation. We also show that oligomerization-defective CCD3 mutants fail in centrosomal localization and centriole linkage, suggesting that rootletin oligomerization may be important for its function.
Identification of a Structurally Dynamic Domain for Oligomer Formation in Rootletin.,Ko D, Kim J, Rhee K, Choi HJ J Mol Biol. 2020 Jun 12;432(13):3915-3932. doi: 10.1016/j.jmb.2020.04.012. Epub, 2020 Apr 20. PMID:32325071[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ko D, Kim J, Rhee K, Choi HJ. Identification of a Structurally Dynamic Domain for Oligomer Formation in Rootletin. J Mol Biol. 2020 Jun 12;432(13):3915-3932. PMID:32325071 doi:10.1016/j.jmb.2020.04.012
