TY - JOUR
T1 - A molecular mechanism for the procentriole recruitment of Ana2
AU - McLamarrah, Tiffany A.
AU - Speed, Sarah K.
AU - Ryniawec, John M.
AU - Buster, Daniel W.
AU - Fagerstrom, Carey J.
AU - Galletta, Brian J.
AU - Rusan, Nasser M.
AU - Rogers, Gregory C.
N1 - Funding Information:
This work was supported by the Division of Intramural Research at the National Institutes of Health/National Heart, Lung, and Blood Institute (1ZIAHL006104) to N.M. Rusan. G.C. Rogers is grateful for support from National Cancer Institute P30 CA23074 and National Institute of General Medical Sciences R01s GM110166 and GM126035 as well as National Institutes of Health grant 1S10OD019948-0. The authors declare no competing financial interests.
Funding Information:
This work was supported by the Division of Intramural Research at the National Institutes of Health/National Heart, Lung, and Blood Institute (1ZIAHL006104) to N.M. Rusan. G.C. Rogers is grateful for support from National Cancer Institute P30 CA23074 and National Institute of General Medical Sciences R01s GM110166 and GM126035 as well as National Institutes of Health grant 1S10OD019948-0.
Publisher Copyright:
© 2019 McLamarrah et al. This article is distributed under the terms of an Attribution-Noncommercial-Share Alike-No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
PY - 2020/2/3
Y1 - 2020/2/3
N2 - During centriole duplication, a preprocentriole forms at a single site on the mother centriole through a process that includes the hierarchical recruitment of a conserved set of proteins, including the Polo-like kinase 4 (Plk4), Ana2/STIL, and the cartwheel protein Sas6. Ana2/STIL is critical for procentriole assembly, and its recruitment is controlled by the kinase activity of Plk4, but how this works remains poorly understood. A structural motif called the G-box in the centriole outer wall protein Sas4 interacts with a short region in the N terminus of Ana2/STIL. Here, we show that binding of Ana2 to the Sas4 G-box enables hyperphosphorylation of the Ana2 N terminus by Plk4. Hyperphosphorylation increases the affinity of the Ana2-G-box interaction, and, consequently, promotes the accumulation of Ana2 at the procentriole to induce daughter centriole formation.
AB - During centriole duplication, a preprocentriole forms at a single site on the mother centriole through a process that includes the hierarchical recruitment of a conserved set of proteins, including the Polo-like kinase 4 (Plk4), Ana2/STIL, and the cartwheel protein Sas6. Ana2/STIL is critical for procentriole assembly, and its recruitment is controlled by the kinase activity of Plk4, but how this works remains poorly understood. A structural motif called the G-box in the centriole outer wall protein Sas4 interacts with a short region in the N terminus of Ana2/STIL. Here, we show that binding of Ana2 to the Sas4 G-box enables hyperphosphorylation of the Ana2 N terminus by Plk4. Hyperphosphorylation increases the affinity of the Ana2-G-box interaction, and, consequently, promotes the accumulation of Ana2 at the procentriole to induce daughter centriole formation.
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U2 - 10.1083/jcb.201905172
DO - 10.1083/jcb.201905172
M3 - Article
C2 - 31841145
AN - SCOPUS:85076576834
SN - 0021-9525
VL - 219
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 2
ER -