Tavernier N , Thomas Y , Vigneron S , Maisonneuve P , Orlicky S , Mader P , Regmi SG , Van Hove L , Levinson NM , Gasmi-Seabrook G , Joly N , Poteau M , Velez-Aguilera G , Gavet O , Castro A , Dasso M , Lorca T , Sicheri F , Pintard L .

FDN 143277 CIHR, FRN 414829 CIHR, MFE 152464 CIHR, R33 CA246363 NCI NIH HHS

	Fig. 1: In vitro reconstitution of a minimal system recapitulating T-loop phosphorylation of Plk1 by Bora and AURKA. a Domain architecture of Homo sapiens AURKA, Bora, and Plk1. The positions of the T-loop phospho-regulatory sites of AURKA (T288) and Plk1 (T210) are indicated. Cy motifs in Bora correspond to Cyclin-binding motifs that mediate substrate targeting. b Two-step in vitro reconstitution of T-loop phosphorylation on T210 of Plk1 (pT210) by AURKA and Bora1–224. In step 1, Bora is phosphorylated by CyclinA2-Cdk2 kinase (yielding pBora). In step 2, phosphorylated Bora from the reaction mix in step 1 is incubated with AURKA and the catalytically dead mutant Plk1K82R in full-length (FL), polo-box domain deleted (∆PBD), or kinase domain-only (KD) forms. During step 2, AURKA phosphorylates Plk1 (noted pT210 Plk1K82R) and Bora or pBora (noted ppBora). c Western blot analysis of kinase reactions carried out with Bora1–224 phosphorylated (+) or not (−) by CyclinA2-Cdk2 (step 1) in the presence of Plk1K82R (FL or ∆PBD or KD) and AURKA (step 2). Schematics of the Plk1 constructs used as substrates are shown at bottom. Blots were probed with antibodies to Bora, AURKA, and phosphoT210 Plk1 or pan Plk1 as indicated (from top to bottom). Note that pBora phosphorylated by AURKA displays slower migration on SDS-PAGE compared to pBora phosphorylated only by CyclinA2-Cdk2. In the blot performed with the anti-pT210 Plk1 antibody, the asterisk denotes cross reactivity with the pT288 residue of AURKA.
	Fig. 2: Bora is an intrinsically disordered protein that binds AURKA.a NMR analysis of the binding interaction between non-phosphorylated 15N-labeled Bora (15N-Bora) and unlabeled AURKA and Plk1. On the left, superimposed 1H-15N HSQC spectra of 15N-Bora alone in black with 15N-Bora in red in the presence of two moles equivalents [1:2] of Plk1 KD. On the right, 15N-Bora alone in black with 15N-Bora in blue in the presence of two moles equivalents [1:2] of AURKA. b NMR analysis of the binding interaction between CyclinA2-Cdk2 phosphorylated 15N-Bora and unlabeled AURKA and Plk1. On the left, superimposed 1H-15N HSQC spectra of phosphorylated 15N-Bora alone in black with phosphorylated 15N-Bora in red in the presence of two moles equivalents [1:2] of Plk1 KD. On the right, phosphorylated 15N-Bora alone in black with phosphorylated 15N-Bora in blue in the presence of two moles equivalents [1:2] of AURKA. c Pull-down experiments between immobilized biotinylated AVI-tagged Bora1–224 (bAVI-Bora1–224) or biotinylated AVI-tagged pBora1–224 and AURKA (left panel), Plk1 KD (middle panel), or a mix of AURKA and Plk1 KD (right panel). d, e SPR binding analysis of immobilized Bora1–224 (d) and pBora1–224 (e) to AURKAWT. Kd values represent mean values, n = 2. Representative profiles shown are from one experiment. See Supplementary Fig. 2d, e, respectively, for sensogram traces.
	Fig. 3: phospho-Bora activates dephospho-AURKA and its mimic AURKAT288V. a Two-step in vitro reconstitution of T-loop phosphorylation on T210 of Plk1 KD (pT210) by AURKA WT, AURKA T-loop mutant (T288V), dephosphorylated AURKA (WTdephos), or catalytically dead AURKAD274N mutant and the activator Bora1–224. In step 1, Bora is phosphorylated (+) or not (−) by CyclinA2-Cdk2 kinase. In step 2, phosphorylated Bora1–224 from the reaction mix in step 1 is incubated with AURKA (in the indicated forms) and the kinase domain KD of catalytically dead Plk1K82R. b Western blot analysis of kinase reactions carried out with Bora1–224 phosphorylated (+) or not (−) by CyclinA2-Cdk2 (step 1) in the presence of Plk1K82R KD and the indicated forms of AURKA, namely WT phosphorylated, WT dephosphorylated, T288V mutant, or D274N mutant (step 2). Blots were probed with antibodies to Bora, AURKA, and phosphoT210 Plk1 or pan Plk1 as indicated (from top to bottom). In the blot performed with the anti-pT210 Plk1 antibody, the asterisk denotes the cross reactivity with the pT288 residue of AURKAWT. c, d Activation of AURKAWT (c) or AURKAT288V (d) kinase activity by Bora1–224 and pBora1–224 as assessed using the ADP-Glo assay and Kemptide substrate. Displayed data points and EC50 values represent the average luminescence for each reaction condition with standard deviations of the mean as error bars (n = 3 independent experiment samples). RLU: relative light unit. ND: not determined. Reaction results carried out in the absence of Kemptide are shown in Supplementary Fig. 3c, d. e, f SPR binding analysis of immobilized Bora1–224 (e) and pBora1–224 (f) to AURKAT288V. Kd values represent mean values, n = 2. Representative profiles shown are from one experiment. See Supplementary Fig. 3e, f, respectively, for sensogram traces.
	Fig. 4: AURKAT288V supports AURKA function in maintaining the mitotic state in CSF-arrested Xenopus oocytes. a In the ovary, oocytes are arrested in prophase of meiosis I. At the time of ovulation and upon hormone stimulation (progesterone), oocytes re-enter into meiosis and reach the second meiotic division where they arrest in metaphase II, awaiting fertilization (CSF arrest). Upon Gwl immunodepletion (∆Gwl in red), the extracts exit the “mitotic state”. Complementation of the extract with recombinant hyperactive GwlK72M kinase (+GwlK72M in green) restores the mitotic state, if the extracts contain a functional Bora, AURKA, Plk1 pathway. GVBD: germinal vesicle breakdown. The green and red area represents the high and low CyclinB-Cdk1 (MPF) activity. b Network representing the pathways controlling Cyclin-Cdk activity and maintaining the “mitotic state” in CSF-arrested Xenopus egg extracts. c Flow chart of the experimental approach used to test the functionality of AURKA mutants in maintaining the “mitotic state” in CSF-arrested Xenopus oocytes extracts. Endogenous AURKA and Gwl were sequentially immunodepleted from CSF egg extracts and then complemented with recombinant human AURKAWT, catalytically dead AURKAD274N, or downregulated mimic AURKAT288V and hyperactive GwlK72M kinase (K72M) (top panel). CSF extracts non-depleted or sequentially depleted of AURKA (∆AURKA) and then Greatwall (∆Gwl) were separated by SDS-PAGE and analyzed by Western blot using Xenopus Gwl and AURKA antibodies. Asterisks denote non-specific bands. d CSF egg extracts sequentially depleted of AURKA (∆AURKA) and then Gwl (∆Gwl) were supplemented at time 0 with recombinant AURKAWT, or catalytically dead AURKAD274N or AURKAT288V in the presence of hyperactive GwlK72M. A fraction of the extracts was collected at the indicated time-points (0, 20, 40, 60, 90 min) and analyzed by Western blot using specific antibodies to monitor the levels of huGreatwall, Hu/Xe AURKA, Plk1, Cdc25, as well as the phosphorylation of Plx1 on T201 (pPlk1), PP1 phosphatase on T320 (pPP1), and Cdk on Y15 (pTyr). The green and red area represents the high and low CyclinB-Cdk1 (MPF) activity (“mitotic state”).
	Fig. 5: Bora contains Tpx2-like motifs and a unique phosphosite required for its activation function on AURKA in vitro. a Schematic of Bora1–224 highlighting ten S/T-P consensus sites that are phosphorylatable by the proline-directed kinases Cyclin-Cdk or ERK. Residue position of the phospho-sites are indicated and highlighted by the letter P (above). Also highlighted are two Cyclin-binding motifs (Cy, violet) and two Tpx2-like motifs 1 and 2 (green). The boundaries of the different Bora fragments analyzed in b–d, are indicated. The most essential phospho-site S112 is highlighted by a large P. b Western blot analysis of 2-step kinase reactions carried out with the indicated Bora fragments phosphorylated (+) or not (−) by the ERK kinase (step 1) in the presence of Plk1K82R KD substrate and AURKAWT or AURKAT288V (step 2). Blots were probed with antibodies to Bora, AURKA, and phosphoT210 Plk1 or pan Plk1 as indicated (from top to bottom). c Alignments of Bora motifs M1 and M2 with Tpx2 motifs responsible for binding to AURKA. Essential residue numbers in Tpx2 responsible for binding AURKA are highlighted in red below the alignments. The corresponding residue numbers in Bora are highlighted in red above the alignments. Also shown is a phospho-motif M3 in Bora not conserved in Tpx2. d Western blot analysis of kinase reactions carried out with the indicated Bora18–120 mutants (S27A and T52A plus/minus mutations within motifs M1 or M2) phosphorylated (+) or not (−) by the ERK kinase (step 1) in the presence of Plk1K82R KD and AURKAWT or AURKAT288V (step 2). Blots were probed with antibodies to Bora, AURKA, and phosphoT210 Plk1 or pan Plk1 as indicated (from top to bottom). Note that the Bora18–120 [S27A T52A F103D F104D] mutant was not recognized by our Bora antibody but Coomassie staining of the step1 reaction (bottom panel of step 1) revealed the presence of the protein at the expected size.
	Fig. 6: Bora and Tpx21–43 compete for AURKA binding. a Schematics of a competitive displacement binding assay using fluorescein-labeled Tpx21–43 (FITC-Tpx21–43) as a probe. Complex formation between FITC-labeled Tpx21–43 polypeptide and AURKA followed by the disassembly of the FITC-Tpx21–43/AURKA complex by increasing amount of competitor (cold Tpx21–43, Bora, or pBora) was monitored by fluorescence polarization. b Binding of fluorescein-labeled Tpx21–43 polypeptide to AURKAWT assessed by monitoring the fluorescence polarization signal in the presence of increasing concentrations of AURKAWT. Kd value represents mean value with standard deviations of the mean as error bars (n = 3 independent experiment samples). c Competitive binding assay where fluorescein-labeled Tpx21–43 polypeptide in complex with AURKAWT is displaced by increasing amount of competitor (cold Tpx21–43, Bora1–224, or pBora1–224) and monitored by fluorescence polarization signal. Displayed data points and the half maximal inhibitory concentration (IC50) value represent the average fluorescence polarization for each reaction conditions with standard deviations of the mean as error bars (n = 3 independent experiment samples). ND: not determined. d Binding of fluorescein-labeled Tpx21–43 polypeptide to AURKAT288V assessed by monitoring the fluorescence polarization signal in the presence of increasing concentrations of AURKAT288V. Kd value represents mean value with standard deviations of the mean as error bars (n = 3 independent experiment samples). e, f Competitive binding assay where fluorescein-labeled Tpx21–43 polypeptide in complex with AURKAT288V is displaced by increasing amount of cold Tpx2, Bora1–224, or pBora1–224 competitor (e), or by increasing amounts of cold pBora1–224, pBora18–120, or the indicated pBora18–120 mutants in the M1 and M2 motifs. Data presented as in c. g Activation of AURKAWT ATPase activity by Bora1–224, pBora1–224, and Tpx21–43 as assessed using the ADP-Glo assay with Kemptide substrate. Displayed data points and EC50 values represent the average luminescence for each reaction condition with standard deviations of the mean as error bars (n = 3 independent experiment samples). RLU: relative light unit. h Activation of AURKAT288V ATPase activity by Bora1–224, pBora1–224, and Tpx21–43 as assessed using the ADP-Glo assay with Kemptide substrate. Data presented as in g. i Activity of the AURKAT288V/pBora1–224 complex in the presence of increasing concentration of competitor Tpx21–43 or Bora1–224 assessed using the ADP-Glo assay in the presence of Kemptide substrate. Displayed data points and the half maximal inhibitory concentration (IC50) value represent the average fluorescence luminescence for each reaction conditions with standard deviations of the mean as error bars (n = 3 independent experiment samples). ND: not determined.
	Fig. 7: Bora binds AURKA through two Tpx2-like motifs that position a phospho-motif in the kinase active site. a Zoom-in view of the binding interface between Tpx2 and AURKA (PDB: 1OL5). The T-loop phospho-residue Thr288, sulfate ion (yellow), and the phospho-T-loop and sulfate ion coordinating residues of AURKA (H176, R180, R255, and R286) are highlighted in stick representation. b Binding of fluorescein-labeled Tpx21–43 polypeptide to AURKA mutants assessed by monitoring the fluorescence polarization signal in the presence of increasing concentrations of AURKA mutants. Kd values represent mean value with standard deviations of the mean as error bars (n = 3 independent experiment samples). c Western blot analysis of 2-step kinase reactions carried out with Bora18-120 [S27A T52A] phosphorylated (+) or not (−) by the ERK kinase (step 1) in the presence of Plk1K82R KD (substrate) and AURKAWT or mutated versions as indicated (step 2). Blots were probed with antibodies to Bora, AURKA, and phosphoT210 Plk1 or pan Plk1 as indicated (from top to bottom). d Competitive displacement of fluorescein-labeled Tpx21–43 from the indicated AURKA mutants by increasing concentrations of pBora1–224 as monitored by fluorescence polarization. Displayed data points and the half maximal inhibitory concentration (IC50) value represent the average normalized fluorescence polarization signal for each reaction conditions (starting binding signal = 100%, end titration binding signal =0%) (n = 3 independent experiment samples). e Theoretical/illustrative model of pBora binding to the kinase domain of AURKA. AURKA is shown in gray surface with helix αC highlighted in yellow. Bora motifs M1 (blue) and M2 (purple) were modeled by two corresponding motifs from Tpx2 and the phospho-motif M3 (pink) was modeled by the TSS motif from phospho-INCENP
	Fig. 8: Tpx2-like motifs and Serine 112 phosphorylation are essential for Bora function in mitotic entry in Xenopus egg extracts. a Schematic for the structure–function analysis of Bora in mitotic entry in Xenopus egg extracts. Interphase extracts (red) were depleted with Bora antibodies and 30 min later supplemented with Bora fragments (pre-phosphorylated by the ERK kinase) and with the recombinant GwlK72M hyperactive kinase to force mitotic entry. Samples were collected at different time-points and analyzed by Western blot (0, 20, 40, 60 min) using mitotic markers to determine whether the extracts enter into mitosis (green) or not. The Western blot shows endogenous Bora levels before (Input) and after (Sn: supernatant) immunodepletion (Ip) from Xenopus egg extracts. b Interphase extracts were immunodepleted using anti-Bora antibodies and 30 min later supplemented with a recombinant hyperactive GwlK72M and Bora1–224 (lanes 2–5), Bora35–157 (lanes 6–9), Bora1–224 (lanes 11–14), Bora18–157 [S27A T52A] (lanes 15–18), Bora18–120 [S27A T52A] (lanes 19–22). A fraction of the extracts was collected at the indicated time-points (0, 20, 40, 60 min) and analyzed by Western blot using specific antibodies to monitor the levels of huGwl, ERK, Plk1, huBora and phosphorylation of Plx1 on T201 (pPlk1), PP1 phosphatase on threonine 320 (pPP1), Cdk on Tyr15 (pTyr), and ERK on Thr202 and Tyr204. The green and red areas at bottom represent high and low CyclinB-Cdk1 (MPF) activity periods. c Interphase extracts were immunodepleted using anti-Bora antibodies and 30 min later supplemented with recombinant hyperactive Gwl (GwlK72M) and Bora18-120 [S27A T52A] (lanes 2–5), Bora18–120 [S27A T52A F25D Y31D] (lanes 6–9), Bora18-120 [S27A T52A F103D F104D] (lanes 10–13). A fraction of the extracts was collected at the indicated time-points (0, 20, 40, 60 min) and analyzed by Western blot using specific antibodies to monitor the levels of Gwl, ERK, Plk1, and Bora as well as phosphorylation of Plx1 on T201 (pPlk1), PP1 phosphatase on threonine 320 (pPP1), and Cdk on Tyr15 (pTyr). The green and red areas at bottom represent high and low CyclinB-Cdk1 (MPF) activity periods.
	Fig. 9: S112 residue and Tpx2-like motifs are essential for Bora function during the mammalian cell cycle. a Schematic for the structure–function analysis of Bora during the mammalian cell cycle. Endogenous Bora located on chromosome (Chr) XIII was C-terminally tagged with Neongreen (NG) and the Auxin-Inducible degron (AID) in DLD1 cells constitutively expressing the Tir1 subunit of the SCFTIR1 E3-ligase. A wild-type or a mutant copy of untagged Bora driven by the doxycycline promoter (pTRE3G) was inserted on Chr XIX of the same cells using CRISPR/Cas9 genome editing. Doxycycline promotes expression of untagged wild-type or mutant Bora, while Auxin induces SCFTIR1-mediated proteasome degradation of Bora-NG-AID resulting in a Bora knockdown. b Workflow used to follow the progression of the cells through the cell cycle. Expression of BoraWT or the indicated mutants were induced with doxycycline during the second thymidine block. Bora-NG-AID was then depleted at the time of release from DTB using Auxin. Cells were collected 10 and 13 h after DTB release for Western blot and FACS analyses. c Histogram plots showing the cell cycle distributions (percentage of cells in G1, S, and G2/M) for DLD1-Bora-NG-AID cell lines, expressing either BoraWT or Bora[S41A S112A S137A] and treated as outlined in b. AS: Asynchronous cells; Ctrl: non-treated; A: Auxin-treated cells; A/D: Doxycyclin + Auxin-treated cells. d Box plots indicate median (middle line) and min max (Wiskers) showing the quantified rescue index (RI) for each DLD1 Bora-NG-AID cell line expressing BoraWT (in dark green) or the indicated mutants: Bora[S41A S112A S137A] (in red), BoraS41A (in blue), BoraS112A (in orange), BoraS137A (in green), Bora∆35 (in magenta), Bora[F25D Y31D] (in pink), and Bora[F103D F104D] (in purple) assessed 10 (first column) and 13 (second column) hours after DTB release; n indicates the number of replicates. e Western blot analysis of protein lysates from a DLD1-Bora-NG-AID cell line expressing BoraWT or the indicated mutants 10 h after DTB release as depicted in b, c, and d. Bora, pT210-Plk1, and panPlk1 antibodies were used for these analyses (from top to bottom). (−) Asynchronous cells.

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