Nwagbara BU , Faris AE , Bearce EA , Erdogan B , Ebbert PT , Evans MF , Rutherford EL , Enzenbacher TB , Lowery LA .

R00 MH095768 NIMH NIH HHS

	FIGURE 1:. TACC3 protein is expressed within embryonic neuronal growth cones and promotes axon outgrowth. (A–F) Immunostaining with antibodies to TACC3 (A) and tubulin (B) in cultured embryonic neural crest cells confirm that TACC3 is enriched at the centrosome (C, A′–C′), in addition to being present in puncta throughout the cell. (D–F) TACC3 antibody also strongly stains growth cones. Scale bar, 5 μm. (G) Western blot showing that a morpholino (MO) targeted against TACC3 results in 50% knockdown (KD) by 2 d postfertilization. Bar graph depicts densito­metry of blot shown; however, similar results were obtained with >20 individual Western blots (unpublished data). (H–I) Axon outgrowth parameters after 24 h in culture were quantified in control and TACC3 KD conditions. (H) The numbers of axons per neural tube explant were counted from three independent experiments. (I) The distance from explant to growth cone was measured to calculate the length of axons from three independent experiments. (J–K) Representative phase contrast microscopy images of axons from control and TACC3 KD. (L) Western blot showing that TACC3 levels are increased (overexpressed [OE]) 2 d after injecting embryos with TACC3 mRNA. Bar graph depicts densitometry of blot shown; however, similar results were obtained with >20 individual Western blots (unpublished data). Note that the TACC3 blot in L was exposed for a shorter amount of time than the one in G, which explains the fainter control band in L. (M, N) Axon outgrowth parameters after 18 h in culture were quantified in control and TACC3 OE conditions. (O–P) Representative phase contrast microscopy images of axons from control and TACC3 OE. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. **p <0.01, ***p <0.001; n.s., not significant. Bar, 50 μm (J, K, O, P).
	FIGURE 2:. TACC3 regulates MT dynamics in X. laevis growth cones and neural crest cells. (A–C) Representative micrographs of EB1-GFP comets in control (A), TACC3 KD (B), and TACC3 OE (C) conditions. See Figure 2 Supplemental Movies S1–S4. Bar, 5 μm. (D–F) Quantification of MT growth track parameters in cultured embryonic neuronal growth cones (GC) after TACC3 manipulation. EB1-GFP localizes to the ends of growing MTs and is thus a marker for MT polymerization. Automated tracking of EB1-GFP comets calculate MT growth-track velocity (D), MT growth-track lifetime (E), and MT growth-track length (F). Examples of actual mean values for a single experiment: GC MT velocity, control, 6.4 μm/min; TACC3 KD, 5.7 μm/min; TACC3 OE, 7.1 μm/min. GC MT lifetime, control, 12.6 s; KD, 13.3 s; OE, 14.1 s. GC MT length, control, 1.4 μm; KD, 1.3 μm; OE, 1.7 μm. NCC MT velocity, control, 7.5 μm/min; KD, 6.0 μm/min; OE, 8.5 μm/min. NCC MT lifetime, control. 11.4 s; KD. 13.0 s; OE, 12.1 s. NCC MT length, control, 1.3 μm; KD, 1.3 μm; OE, 1.8 μm. For each independent experiment (six were performed in total), measurements of MT parameters were normalized to their respective experimental control means due to the significant day-to-day fluctuations in control MT dynamics (in part, due to room temperature changes). Control data represent the means of 44 growth cones, representing a total of 1228 analyzed tracks; TACC3 KD represents 49 growth cones with 964 tracks; TACC3 OE represents 24 growth cones with 524 tracks. (G–I) Quantification of MT growth-track parameters in cultured embryonic neural crest cells. Control data represent the means of 20 neural crest cells, representing a total of 2876 analyzed tracks; TACC3 KD represents 13 cells with 1313 tracks; TACC3 OE represents 10 cells with 1386 tracks. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. *p <0.05, **p <0.01, ***p <0.001; ns, not significant.
	FIGURE 3:. TACC3 can act as a +TIP in neuronal growth cones and neural crest cells. (A–C) Expression of mKate2-tubulin (A), GFP-TACC3 (B), and merge (C) in living growth cone (gc). See Figure 3 Supplemental Movie 1. (A′–C′) Magnified time-lapse montages of the boxed regions in A–C shows that GFP-TACC3 localizes to growing MT plus ends. (D) Fluorescence intensity profile of line-scan average from 30 MT plus ends in growth cones. (E) Histogram depicting the distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs in growth cones. (F) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. (G–I) Expression of mKate2-tubulin (G), GFP-TACC3 (H), and merge (I) in living neural crest cell (ncc). See Figure 3 Supplemental Movie 2. (G′–I′) Magnified views of the boxed regions in G–I. See Figure 3 Supplemental Movie 3. (G′′–I′′) Magnified time-lapse montages of the boxed regions in G′–I′. (J) Fluorescence intensity profile of line-scan average from 45 MT plus ends in neural crest cells. (K) Distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs. (L) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. Bar, 1 μm.
	FIGURE 4:. TACC3 can act as a +TIP in nonneuronal embryonic cells. (A–C) Expression of mKate2-tubulin (A), GFP-TACC3 (B), and merge (C) in cultured fibroblasts derived from embryonic somitic mesoderm. See Figure 4 Supplemental Movie 1. (A′–C′) Magnified views of the boxed regions in A–C. See Figure 4 Supplemental Movie 2. (A′′–C′′) Magnified time-lapse montages of the boxed regions in A′–C′. (D) Time-lapse montage of another MT in the process of undergoing catastrophe, with GFP-TACC3 localizing. (E) Fluorescence intensity profile of line-scan average from 43 MT plus ends. (F) Histogram depicting the distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs. (G) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. (H) Quantification of mean fluorescence intensity of 4 × 4 pixel square of GFP-TACC3 accumulation on the ends of MTs, when visible. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. Bar, 1 μm.
	FIGURE 5:. The TACC domain is necessary but not sufficient for MT plus end tracking by TACC3. (A) Schematic representation of GFP-tagged TACC3 proteins and deletion constructs, and designation of whether the protein tracks along growing MT plus ends. The amino acid residue numbers refer to those in full-length X. laevis TACC3 from GenBank accession number NP_001081964.1. Conserved domains of TACC3 include an N-terminal, conserved region, a C-terminal, highly conserved TACC domain, and a short, highly conserved region, which is located before the TACC domain. The TACC domain consists of two coiled-coil (CC) domains, CC1 and CC2. The TACC domain is necessary for localization to the centrosome (Gergely et al., 2000b; Peset et al., 2005) and interaction with XMAP215 family members (Lee et al., 2001; Thakur et al., 2014). (B–M) Expression of GFP-tagged TACC3 constructs (B, E, H, K, N), mKate2-EB1 (to identify MT plus ends; C, F, I, L, O), and merged images of both channels (D, G, J, M, P). Plus end accumulation is apparent in B and E but not H, K, or N. Images in K–M are from the edge of a neural crest cell, whereas all others are growth cones. See Figure 5 Supplemental Movies 1–5. Bar, 5 μm.
	FIGURE 6:. TACC3 localization on MT plus ends is more distal than EB1 and overlaps with XMAP215. (A–C) Representative time-lapse montage of GFP-TACC3 (A) and mKate2-EB1 (B) accumulation on growing MT plus end. MT is growing to the right. Merged image (C) highlights the spatial arrangement between GFP-TACC3 and mKate2-EB1 localizations. These images were compiled by translating the TACC3 channel on the x-axis, after calculating the frame-to-frame velocity of the growing MT plus end, in order to account for the 1-s time delay between channels, for each examined MT (using ImageJ Translate function). To further confirm correct translation, uncorrected time-lapse colocalizations were examined with both combinations of imaging—red channel first, green channel second; then green channel first, red channel second. (D) Fluorescence intensity profiles of GFP-TACC3 and mKate2-EB1. GFP-TACC3 and mKate2-EB1 signals from 12 individual MTs were quantified by intensity line scans to present the relative fluorescence intensity profiles, with the plus end of the MT toward the right. The highest-intensity peak of GFP-TACC3 is ∼0.5 μm distal to the peak of mKate2-EB1. (E–G) Representative time-lapse montage of mKate2-TACC3 (E) and XMAP215-GFP (F) accumulation on growing MT plus end. MT is growing to the right. Merged image (G) shows that mKate2-TACC3 and XMAP215-GFP localizations overlap. (H) Fluorescence intensity profiles of mKate2-TACC3 and XMAP215-GFP. mKate2-TACC3 and XMAP215-GFP signals from 11 individual MTs were quantified by intensity line scans to present the relative fluorescence intensity profiles. Note that peak intensities of mKate2-TACC3 and XMAP215-GFP closely align. Bar, 0.5 μm.
	FIGURE 7:. TACC3 and XMAP215 levels affect each other's protein stability and localization to MT plus ends. (A, B) Representative Western blots showing levels of TACC3 and XMAP215 after TACC3 KD (A) or overexpression (B). The graphs in A′ and B′ are compilations of seven and six individual Western blot experiments, respectively. (C, D) Representative Western blots showing levels of XMAP215 and TACC3 after XMAP215 KD (C) or overexpression (D). The graphs in C′ and C′′ are from six Western blot experiments, and D′ and D′′ are from three experiments. Bars in graphs of Western densitometry denote SE. A Kruskal–Wallis test was performed to assess significance of differences in Western blot densitometry. *p <0.05. (E) Quantification of fluorescence intensity levels of XMAP215-GFP on MT plus ends in control, TACC3 KD, and TACC3 OE conditions, normalized to cytoplasmic levels. Data represent analysis of ∼100 individual MTs from numerous growth cones for each condition. (F) Quantification of fluorescence intensity levels of GFP-TACC3 on MT plus ends in control and XMAP215 KD conditions, normalized to cytoplasmic levels. Data represent analysis of 149 and 151 individual MTs from numerous growth cones per condition. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. **p <0.01, ***p <0.001; ns, not significant.
	FIGURE 8:. Cartoon schematic of proposed model of TACC3 interaction at MT plus ends. Both TACC3 (red) and XMAP215 (green) bind to the extreme MT plus end. TACC3 and XMAP215 are known to interact with each other through their C-terminal domains (Lee et al., 2001; Thakur et al., 2014), whereas XMAP215 can bind to tubulin dimers through its N-terminal TOG domains (Widlund et al., 2011). TACC3 and XMAP215 complex formation in the cytoplasm may serve to stabilize each other (Bellanger and Gonczy, 2003; Figure 7), and TACC3 interaction with XMAP215 may promote more efficient binding of the complex to MTs in order to drive MT polymerization activity (Kinoshita et al., 2005; Peset et al., 2005). It is unknown whether TACC3 can bind to MT plus ends directly or only through XMAP215 (as depicted here). EB1 (orange) binding to MT plus ends is behind TACC3 and XMAP215 (Figure 6). Not drawn to scale.
	FIGURE 1:. TACC3 protein is expressed within embryonic neuronal growth cones and promotes axon outgrowth. (A–F) Immunostaining with antibodies to TACC3 (A) and tubulin (B) in cultured embryonic neural crest cells confirm that TACC3 is enriched at the centrosome (C, A′–C′), in addition to being present in puncta throughout the cell. (D–F) TACC3 antibody also strongly stains growth cones. Scale bar, 5 μm. (G) Western blot showing that a morpholino (MO) targeted against TACC3 results in 50% knockdown (KD) by 2 d postfertilization. Bar graph depicts densito­metry of blot shown; however, similar results were obtained with >20 individual Western blots (unpublished data). (H–I) Axon outgrowth parameters after 24 h in culture were quantified in control and TACC3 KD conditions. (H) The numbers of axons per neural tube explant were counted from three independent experiments. (I) The distance from explant to growth cone was measured to calculate the length of axons from three independent experiments. (J–K) Representative phase contrast microscopy images of axons from control and TACC3 KD. (L) Western blot showing that TACC3 levels are increased (overexpressed [OE]) 2 d after injecting embryos with TACC3 mRNA. Bar graph depicts densitometry of blot shown; however, similar results were obtained with >20 individual Western blots (unpublished data). Note that the TACC3 blot in L was exposed for a shorter amount of time than the one in G, which explains the fainter control band in L. (M, N) Axon outgrowth parameters after 18 h in culture were quantified in control and TACC3 OE conditions. (O–P) Representative phase contrast microscopy images of axons from control and TACC3 OE. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. **p <0.01, ***p <0.001; n.s., not significant. Bar, 50 μm (J, K, O, P).
	FIGURE 2:. TACC3 regulates MT dynamics in X. laevis growth cones and neural crest cells. (A–C) Representative micrographs of EB1-GFP comets in control (A), TACC3 KD (B), and TACC3 OE (C) conditions. See Figure 2 Supplemental Movies S1–S4. Bar, 5 μm. (D–F) Quantification of MT growth track parameters in cultured embryonic neuronal growth cones (GC) after TACC3 manipulation. EB1-GFP localizes to the ends of growing MTs and is thus a marker for MT polymerization. Automated tracking of EB1-GFP comets calculate MT growth-track velocity (D), MT growth-track lifetime (E), and MT growth-track length (F). Examples of actual mean values for a single experiment: GC MT velocity, control, 6.4 μm/min; TACC3 KD, 5.7 μm/min; TACC3 OE, 7.1 μm/min. GC MT lifetime, control, 12.6 s; KD, 13.3 s; OE, 14.1 s. GC MT length, control, 1.4 μm; KD, 1.3 μm; OE, 1.7 μm. NCC MT velocity, control, 7.5 μm/min; KD, 6.0 μm/min; OE, 8.5 μm/min. NCC MT lifetime, control. 11.4 s; KD. 13.0 s; OE, 12.1 s. NCC MT length, control, 1.3 μm; KD, 1.3 μm; OE, 1.8 μm. For each independent experiment (six were performed in total), measurements of MT parameters were normalized to their respective experimental control means due to the significant day-to-day fluctuations in control MT dynamics (in part, due to room temperature changes). Control data represent the means of 44 growth cones, representing a total of 1228 analyzed tracks; TACC3 KD represents 49 growth cones with 964 tracks; TACC3 OE represents 24 growth cones with 524 tracks. (G–I) Quantification of MT growth-track parameters in cultured embryonic neural crest cells. Control data represent the means of 20 neural crest cells, representing a total of 2876 analyzed tracks; TACC3 KD represents 13 cells with 1313 tracks; TACC3 OE represents 10 cells with 1386 tracks. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. *p <0.05, **p <0.01, ***p <0.001; ns, not significant.
	FIGURE 3:. TACC3 can act as a +TIP in neuronal growth cones and neural crest cells. (A–C) Expression of mKate2-tubulin (A), GFP-TACC3 (B), and merge (C) in living growth cone (gc). See Figure 3 Supplemental Movie 1. (A′–C′) Magnified time-lapse montages of the boxed regions in A–C shows that GFP-TACC3 localizes to growing MT plus ends. (D) Fluorescence intensity profile of line-scan average from 30 MT plus ends in growth cones. (E) Histogram depicting the distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs in growth cones. (F) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. (G–I) Expression of mKate2-tubulin (G), GFP-TACC3 (H), and merge (I) in living neural crest cell (ncc). See Figure 3 Supplemental Movie 2. (G′–I′) Magnified views of the boxed regions in G–I. See Figure 3 Supplemental Movie 3. (G′′–I′′) Magnified time-lapse montages of the boxed regions in G′–I′. (J) Fluorescence intensity profile of line-scan average from 45 MT plus ends in neural crest cells. (K) Distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs. (L) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. Bar, 1 μm.
	FIGURE 4:. TACC3 can act as a +TIP in nonneuronal embryonic cells. (A–C) Expression of mKate2-tubulin (A), GFP-TACC3 (B), and merge (C) in cultured fibroblasts derived from embryonic somitic mesoderm. See Figure 4 Supplemental Movie 1. (A′–C′) Magnified views of the boxed regions in A–C. See Figure 4 Supplemental Movie 2. (A′′–C′′) Magnified time-lapse montages of the boxed regions in A′–C′. (D) Time-lapse montage of another MT in the process of undergoing catastrophe, with GFP-TACC3 localizing. (E) Fluorescence intensity profile of line-scan average from 43 MT plus ends. (F) Histogram depicting the distribution of lengths of detectable GFP-TACC3 localization on the plus ends of MTs. (G) Percentage of MT plus ends with GFP-TACC3 localization for different MT dynamics instability states. (H) Quantification of mean fluorescence intensity of 4 × 4 pixel square of GFP-TACC3 accumulation on the ends of MTs, when visible. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. Bar, 1 μm.
	FIGURE 5:. The TACC domain is necessary but not sufficient for MT plus end tracking by TACC3. (A) Schematic representation of GFP-tagged TACC3 proteins and deletion constructs, and designation of whether the protein tracks along growing MT plus ends. The amino acid residue numbers refer to those in full-length X. laevis TACC3 from GenBank accession number NP_001081964.1. Conserved domains of TACC3 include an N-terminal, conserved region, a C-terminal, highly conserved TACC domain, and a short, highly conserved region, which is located before the TACC domain. The TACC domain consists of two coiled-coil (CC) domains, CC1 and CC2. The TACC domain is necessary for localization to the centrosome (Gergely et al., 2000b; Peset et al., 2005) and interaction with XMAP215 family members (Lee et al., 2001; Thakur et al., 2014). (B–M) Expression of GFP-tagged TACC3 constructs (B, E, H, K, N), mKate2-EB1 (to identify MT plus ends; C, F, I, L, O), and merged images of both channels (D, G, J, M, P). Plus end accumulation is apparent in B and E but not H, K, or N. Images in K–M are from the edge of a neural crest cell, whereas all others are growth cones. See Figure 5 Supplemental Movies 1–5. Bar, 5 μm.
	FIGURE 6:. TACC3 localization on MT plus ends is more distal than EB1 and overlaps with XMAP215. (A–C) Representative time-lapse montage of GFP-TACC3 (A) and mKate2-EB1 (B) accumulation on growing MT plus end. MT is growing to the right. Merged image (C) highlights the spatial arrangement between GFP-TACC3 and mKate2-EB1 localizations. These images were compiled by translating the TACC3 channel on the x-axis, after calculating the frame-to-frame velocity of the growing MT plus end, in order to account for the 1-s time delay between channels, for each examined MT (using ImageJ Translate function). To further confirm correct translation, uncorrected time-lapse colocalizations were examined with both combinations of imaging—red channel first, green channel second; then green channel first, red channel second. (D) Fluorescence intensity profiles of GFP-TACC3 and mKate2-EB1. GFP-TACC3 and mKate2-EB1 signals from 12 individual MTs were quantified by intensity line scans to present the relative fluorescence intensity profiles, with the plus end of the MT toward the right. The highest-intensity peak of GFP-TACC3 is ∼0.5 μm distal to the peak of mKate2-EB1. (E–G) Representative time-lapse montage of mKate2-TACC3 (E) and XMAP215-GFP (F) accumulation on growing MT plus end. MT is growing to the right. Merged image (G) shows that mKate2-TACC3 and XMAP215-GFP localizations overlap. (H) Fluorescence intensity profiles of mKate2-TACC3 and XMAP215-GFP. mKate2-TACC3 and XMAP215-GFP signals from 11 individual MTs were quantified by intensity line scans to present the relative fluorescence intensity profiles. Note that peak intensities of mKate2-TACC3 and XMAP215-GFP closely align. Bar, 0.5 μm.
	FIGURE 7:. TACC3 and XMAP215 levels affect each other's protein stability and localization to MT plus ends. (A, B) Representative Western blots showing levels of TACC3 and XMAP215 after TACC3 KD (A) or overexpression (B). The graphs in A′ and B′ are compilations of seven and six individual Western blot experiments, respectively. (C, D) Representative Western blots showing levels of XMAP215 and TACC3 after XMAP215 KD (C) or overexpression (D). The graphs in C′ and C′′ are from six Western blot experiments, and D′ and D′′ are from three experiments. Bars in graphs of Western densitometry denote SE. A Kruskal–Wallis test was performed to assess significance of differences in Western blot densitometry. *p <0.05. (E) Quantification of fluorescence intensity levels of XMAP215-GFP on MT plus ends in control, TACC3 KD, and TACC3 OE conditions, normalized to cytoplasmic levels. Data represent analysis of ∼100 individual MTs from numerous growth cones for each condition. (F) Quantification of fluorescence intensity levels of GFP-TACC3 on MT plus ends in control and XMAP215 KD conditions, normalized to cytoplasmic levels. Data represent analysis of 149 and 151 individual MTs from numerous growth cones per condition. Box-and-whisker plots indicate the mean (diamond), median, extrema, and quartiles. An unpaired t test was performed to assess significance between conditions. **p <0.01, ***p <0.001; ns, not significant.

Akhmanova, Tracking the ends: a dynamic protein network controls the fate of microtubule tips. 2008, Pubmed

Akhmanova, Tracking the ends: a dynamic protein network controls the fate of microtubule tips. 2008, Pubmed
                     Applegate, plusTipTracker: Quantitative image analysis software for the measurement of microtubule dynamics. 2011, Pubmed
                     Barnard, Differential phosphorylation controls Maskin association with eukaryotic translation initiation factor 4E and localization on the mitotic apparatus. 2005, Pubmed , Xenbase
                     Bellanger, TAC-1 and ZYG-9 form a complex that promotes microtubule assembly in C. elegans embryos. 2003, Pubmed
                     Brouhard, XMAP215 is a processive microtubule polymerase. 2008, Pubmed , Xenbase
                     Cullen, Msps protein is localized to acentrosomal poles to ensure bipolarity of Drosophila meiotic spindles. 2001, Pubmed
                     Engel, Abelson phosphorylation of CLASP2 modulates its association with microtubules and actin. 2014, Pubmed , Xenbase
                     Gergely, D-TACC: a novel centrosomal protein required for normal spindle function in the early Drosophila embryo. 2000, Pubmed
                     Gergely, The TACC domain identifies a family of centrosomal proteins that can interact with microtubules. 2001, Pubmed
                     Giet, Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules. 2002, Pubmed , Xenbase
                     Groisman, CPEB, maskin, and cyclin B1 mRNA at the mitotic apparatus: implications for local translational control of cell division. 2000, Pubmed , Xenbase
                     Gómez, Working with Xenopus spinal neurons in live cell culture. 2003, Pubmed , Xenbase
                     Honnappa, An EB1-binding motif acts as a microtubule tip localization signal. 2009, Pubmed
                     Hur, GSK3 controls axon growth via CLASP-mediated regulation of growth cone microtubules. 2011, Pubmed
                     Kinoshita, Aurora A phosphorylation of TACC3/maskin is required for centrosome-dependent microtubule assembly in mitosis. 2005, Pubmed , Xenbase
                     Le Bot, TAC-1, a regulator of microtubule length in the C. elegans embryo. 2003, Pubmed
                     Lee, The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream of the tyrosine kinase Abl in mediating axon guidance. 2004, Pubmed , Xenbase
                     Lee, Msps/XMAP215 interacts with the centrosomal protein D-TACC to regulate microtubule behaviour. 2001, Pubmed , Xenbase
                     Li, EB1 promotes microtubule dynamics by recruiting Sentin in Drosophila cells. 2011, Pubmed
                     Long, Multiparametric analysis of CLASP-interacting protein functions during interphase microtubule dynamics. 2013, Pubmed , Xenbase
                     Lowery, Growth cone-specific functions of XMAP215 in restricting microtubule dynamics and promoting axonal outgrowth. 2013, Pubmed , Xenbase
                     Lowery, The trip of the tip: understanding the growth cone machinery. 2009, Pubmed , Xenbase
                     Marx, Xenopus cytoplasmic linker-associated protein 1 (XCLASP1) promotes axon elongation and advance of pioneer microtubules. 2013, Pubmed , Xenbase
                     Maurer, EB1 accelerates two conformational transitions important for microtubule maturation and dynamics. 2014, Pubmed
                     Nakamura, Dissecting the nanoscale distributions and functions of microtubule-end-binding proteins EB1 and ch-TOG in interphase HeLa cells. 2012, Pubmed
                     Neukirchen, Cytoplasmic linker proteins regulate neuronal polarization through microtubule and growth cone dynamics. 2011, Pubmed
                     O'Brien, The Xenopus TACC homologue, maskin, functions in mitotic spindle assembly. 2005, Pubmed , Xenbase
                     Peset, The TACC proteins: TACC-ling microtubule dynamics and centrosome function. 2008, Pubmed
                     Peset, Function and regulation of Maskin, a TACC family protein, in microtubule growth during mitosis. 2005, Pubmed , Xenbase
                     Rochlin, Microtubule stability decreases axon elongation but not axoplasm production. 1996, Pubmed
                     Sadek, TACC3 expression is tightly regulated during early differentiation. 2003, Pubmed
                     Samereier, Analysis of Dictyostelium TACC reveals differential interactions with CP224 and unusual dynamics of Dictyostelium microtubules. 2011, Pubmed
                     Shcherbo, Far-red fluorescent tags for protein imaging in living tissues. 2009, Pubmed , Xenbase
                     Sive, Microinjection of Xenopus embryos. 2010, Pubmed , Xenbase
                     Srayko, Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential for long astral and spindle microtubules. 2003, Pubmed
                     Stebbins-Boaz, Maskin is a CPEB-associated factor that transiently interacts with elF-4E. 2000, Pubmed , Xenbase
                     Stepanova, Visualization of microtubule growth in cultured neurons via the use of EB3-GFP (end-binding protein 3-green fluorescent protein). 2003, Pubmed
                     Stout, Using plusTipTracker software to measure microtubule dynamics in Xenopus laevis growth cones. 2014, Pubmed , Xenbase
                     Tanaka, Microtubule behavior in the growth cones of living neurons during axon elongation. 1991, Pubmed , Xenbase
                     Tanaka, The role of microtubule dynamics in growth cone motility and axonal growth. 1995, Pubmed , Xenbase
                     Tessmar, A screen for co-factors of Six3. 2002, Pubmed , Xenbase
                     Thakur, The centrosomal adaptor TACC3 and the microtubule polymerase chTOG interact via defined C-terminal subdomains in an Aurora-A kinase-independent manner. 2014, Pubmed
                     Widlund, XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region. 2011, Pubmed
                     Xie, Cep120 and TACCs control interkinetic nuclear migration and the neural progenitor pool. 2007, Pubmed
                     Yang, DOCK7 interacts with TACC3 to regulate interkinetic nuclear migration and cortical neurogenesis. 2012, Pubmed
                     Zhou, NGF-induced axon growth is mediated by localized inactivation of GSK-3beta and functions of the microtubule plus end binding protein APC. 2004, Pubmed
                     van der Vaart, SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase. 2011, Pubmed
                     van der Vaart, Microtubule plus-end tracking proteins SLAIN1/2 and ch-TOG promote axonal development. 2012, Pubmed