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Cited by 1,676Genetic and Kidney Cyst DiseasesMicrotubule and mitosis dynamicsCystic Fibrosis Research Advances

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The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

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Khalifa, Ahmad Abdelzaher Zaki, Ichikawa, Muneyoshi, Dai, Daniel, Kubo, Shintaroh, Black, Corbin Steven, Peri, Katya, McAlear, Thomas S, Veyron, Simon, Yang, Shun Kai, Vargas, Javier, Bechstedt, Susanne, Trempe, Jean-François, Bui, Khanh Huy·2020·eLife
DOI 10.7554/elife.52760PMC PMC6994238

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Abstract

Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of Chlamydomonas reinhardtii and Tetrahymena thermophila, we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility.

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Figures

Figure 1. The IJ structures of Chlamydomonas and Tetrahymena doublet. (A–D) Surface renderings and schematics of the 48 nm repeat cryo-EM maps of Chlamydomonas (A, B) and Tetrahymena (C, D) doublets viewed from the tip of the cilia. Black arrow indicates longitudinal view in (E), (F) and (G). (E–F) The longitudinal section of the Chlamydomonas doublet at the IJ complex from the inside (E) and outside (F). (G) The longitudinal section of Tetrahymena doublet viewed from the inside. Color scheme: FAP20: dark green; PACRG: gray; FAP52: light green, Y-shaped density: purple; FAP45: yellow green; fMIP-B8B9: orange; Tubulin: light gray; Unknown density: yellow; Rest of MIPs: white; Tether density 1 and 2: red; Tether density 3, pink. Plus and minus ends are indicated by + and - signs. (H) Cross sectional views of the different Tether densities from Chlamydomonas (left) and Tetrahymena (right). In Chlamydomonas, there is a Y-shaped density (purple) that cradles the FAP52 density. The Y-shaped density is absent in Tetrahymena. In Tetrahymena, we observed Tether density 3, which is absent in Chlamydomonas.
Figure 1. The IJ structures of Chlamydomonas and Tetrahymena doublet. (A–D) Surface renderings and schematics of the 48 nm repeat cryo-EM maps of Chlamydomonas (A, B) and Tetrahymena (C, D) doublets viewed from the tip of the cilia. Black arrow indicates longitudinal view in (E), (F) and (G). (E–F) The longitudinal section of the Chlamydomonas doublet at the IJ complex from the inside (E) and outside (F). (G) The longitudinal section of Tetrahymena doublet viewed from the inside. Color scheme: FAP20: dark green; PACRG: gray; FAP52: light green, Y-shaped density: purple; FAP45: yellow green; fMIP-B8B9: orange; Tubulin: light gray; Unknown density: yellow; Rest of MIPs: white; Tether density 1 and 2: red; Tether density 3, pink. Plus and minus ends are indicated by + and - signs. (H) Cross sectional views of the different Tether densities from Chlamydomonas (left) and Tetrahymena (right). In Chlamydomonas, there is a Y-shaped density (purple) that cradles the FAP52 density. The Y-shaped density is absent in Tetrahymena. In Tetrahymena, we observed Tether density 3, which is absent in Chlamydomonas.CC BY · PubMed Central
Figure 1—figure supplement 1. Data related to the doublet structures. (A) Schematics of fractionation of the axoneme in this study. Doublets were split from axoneme, and outside proteins were removed to obtain a simpler sample for cryo-EM. (B) A typical cryo-EM image of Chlamydomonas doublets. (C) Gold-standard Fourier Shell Correlation of the 48 nm repeat and 16 nm repeat doublet maps of Chlamydomonas and Tetrahymena. (D) Local resolution estimation of the 16 nm repeat maps from Chlamydomonas and Tetrahymena using MonoRes. The resolution of the B-tubule in Tetrahymena is lower due to the loss of the IJ PF. (E) The remaining PACRG- and FAP20-like densities in the Tetrahymena doublet structure. (F) Superimposition of the tomographic structure of the intact doublet (EMD-2132) with the 48 nm structure of the Chlamydomonas doublet in this study. The DRC is colored green. (G) Enlarged view of the missing PACRG unit at the IJ PF, where the DRC binds. Bars in E and H denote a length of 5 nm.
Figure 1—figure supplement 1. Data related to the doublet structures. (A) Schematics of fractionation of the axoneme in this study. Doublets were split from axoneme, and outside proteins were removed to obtain a simpler sample for cryo-EM. (B) A typical cryo-EM image of Chlamydomonas doublets. (C) Gold-standard Fourier Shell Correlation of the 48 nm repeat and 16 nm repeat doublet maps of Chlamydomonas and Tetrahymena. (D) Local resolution estimation of the 16 nm repeat maps from Chlamydomonas and Tetrahymena using MonoRes. The resolution of the B-tubule in Tetrahymena is lower due to the loss of the IJ PF. (E) The remaining PACRG- and FAP20-like densities in the Tetrahymena doublet structure. (F) Superimposition of the tomographic structure of the intact doublet (EMD-2132) with the 48 nm structure of the Chlamydomonas doublet in this study. The DRC is colored green. (G) Enlarged view of the missing PACRG unit at the IJ PF, where the DRC binds. Bars in E and H denote a length of 5 nm.CC BY · PubMed Central
Figure 2. 16 nm structure of Chlamydomonas doublet. (A, B) 16 nm repeat structure of Chlamydomonas doublet and model at the IJ region. Tubulin densities are depicted as transparent gray, except in A in which tubulins are shown in dark blue. (C) Atomic model of the IJ complex, consisting of PACRG, FAP20, FAP52 and FAP276. Color scheme: FAP20: dark green; PACRG: gray; FAP52: light green, FAP276: purple; tubulin: transparent gray density. (D, E) Maps and models of PF A1 and B10, and IJ PF illustrating how the IJ PF interacts with tubulins. The views are indicated in the schematics. Dashed boxes indicate the views in (F), (G) and (H). Color scheme: α-tubulin: green; β-tubulin: blue; PACRG: gray; FAP20: dark green; FAP276: purple. (F) Electrostatic surface charge of PACRG, FAP20 and α- and β-tubulins of PF A1. Tubulin surface is negatively charged while the interacting interface of PACRG and FAP20 are positively charged. (G) The interaction of the PACRG with the inter-dimer interface of tubulins from PF B10 is shown. H136 from PACRG is conserved and is likely to take part in the interaction with D127 and C129 from α-tubulin of PF B10. (H) The C-terminus of β-tubulin of PF A1 interacts with PACRG and FAP20. Potential residues involved in the interaction of C-tail of β-tubulin and PACRG and FAP20 are shown. (I) Chlamydomonas PACRG has a long N-terminus 1–117. The N-terminus of Chlamydomonas PACRG (red) forms a stable triple helix arrangement with the core of the protein. This is not observed in the human PACRG (PDB: 6NDU) shown in yellow. In addition, the N-terminus of PACRG going into the wedge between PF A13 and A1.
Figure 2. 16 nm structure of Chlamydomonas doublet. (A, B) 16 nm repeat structure of Chlamydomonas doublet and model at the IJ region. Tubulin densities are depicted as transparent gray, except in A in which tubulins are shown in dark blue. (C) Atomic model of the IJ complex, consisting of PACRG, FAP20, FAP52 and FAP276. Color scheme: FAP20: dark green; PACRG: gray; FAP52: light green, FAP276: purple; tubulin: transparent gray density. (D, E) Maps and models of PF A1 and B10, and IJ PF illustrating how the IJ PF interacts with tubulins. The views are indicated in the schematics. Dashed boxes indicate the views in (F), (G) and (H). Color scheme: α-tubulin: green; β-tubulin: blue; PACRG: gray; FAP20: dark green; FAP276: purple. (F) Electrostatic surface charge of PACRG, FAP20 and α- and β-tubulins of PF A1. Tubulin surface is negatively charged while the interacting interface of PACRG and FAP20 are positively charged. (G) The interaction of the PACRG with the inter-dimer interface of tubulins from PF B10 is shown. H136 from PACRG is conserved and is likely to take part in the interaction with D127 and C129 from α-tubulin of PF B10. (H) The C-terminus of β-tubulin of PF A1 interacts with PACRG and FAP20. Potential residues involved in the interaction of C-tail of β-tubulin and PACRG and FAP20 are shown. (I) Chlamydomonas PACRG has a long N-terminus 1–117. The N-terminus of Chlamydomonas PACRG (red) forms a stable triple helix arrangement with the core of the protein. This is not observed in the human PACRG (PDB: 6NDU) shown in yellow. In addition, the N-terminus of PACRG going into the wedge between PF A13 and A1.CC BY · PubMed Central
Figure 2—figure supplement 1. Atomic models of PACRG, FAP20, FAP52 and FAP276. Atomic model of (A) PACRG, (C) FAP20, (E) FAP52 and (G) FAP276. Illustration of the cryo-EM density quality at selected regions of (B) PACRG, (D) FAP20, (F) FAP52 and (H) FAP276.
Figure 2—figure supplement 1. Atomic models of PACRG, FAP20, FAP52 and FAP276. Atomic model of (A) PACRG, (C) FAP20, (E) FAP52 and (G) FAP276. Illustration of the cryo-EM density quality at selected regions of (B) PACRG, (D) FAP20, (F) FAP52 and (H) FAP276.CC BY · PubMed Central
Figure 3. Interaction between PACRG and FAP20. (A) Consecutive molecules of PACRG and FAP20 in the IJ PF. PACRG and FAP20 form a heterodimer as indicated by brackets. (B) Magnified view of the interacting region of PACRG and FAP20. Residues Q264 and D258 of PACRG form hydrogen bonds with residue T38 and K20 of FAP20, respectively. (C, D) Electrostatic interactions between PACRG and FAP20 illustrated by their surface charge. The dashed boxes in (A, C, D) highlight the interacting loops between PACRG and FAP20 (B). (E) Multiple sequence alignment of PACRG in the regions of FAP20-binding loop. Asterisks indicate residues that are involved in FAP20 binding.
Figure 3. Interaction between PACRG and FAP20. (A) Consecutive molecules of PACRG and FAP20 in the IJ PF. PACRG and FAP20 form a heterodimer as indicated by brackets. (B) Magnified view of the interacting region of PACRG and FAP20. Residues Q264 and D258 of PACRG form hydrogen bonds with residue T38 and K20 of FAP20, respectively. (C, D) Electrostatic interactions between PACRG and FAP20 illustrated by their surface charge. The dashed boxes in (A, C, D) highlight the interacting loops between PACRG and FAP20 (B). (E) Multiple sequence alignment of PACRG in the regions of FAP20-binding loop. Asterisks indicate residues that are involved in FAP20 binding.CC BY · PubMed Central
Figure 3—figure supplement 1. Multiple sequence alignment of FAP20 shows that it is highly conserved.
Figure 3—figure supplement 1. Multiple sequence alignment of FAP20 shows that it is highly conserved.CC BY · PubMed Central
Figure 4. Structure of FAP52 and its interaction with tubulins and PACRG. (A) Structure of FAP52 in a top view from the outside of the B-tubule looking down on the A-tubule. Black arrow indicates the direction of view in (B). (B) Three-point contacts of FAP52 with α-tubulins from PF B9 and B10 and PACRG, indicated by the black dashed boxes. The α-K40 loops are colored red. (C, D) The structure of the α-K40 loop from PF B10. Red dashed boxes indicate the α-K40 loop. (E) Interaction of α-K40 loop of PF B10 with FAP52. FAP52’s K229 is within favorable distance to form hydrogen bonds with the backbone of D39 and T41. Hydrophobic interactions between L226 and I42 and interactions involving R225 are also possible.
Figure 4. Structure of FAP52 and its interaction with tubulins and PACRG. (A) Structure of FAP52 in a top view from the outside of the B-tubule looking down on the A-tubule. Black arrow indicates the direction of view in (B). (B) Three-point contacts of FAP52 with α-tubulins from PF B9 and B10 and PACRG, indicated by the black dashed boxes. The α-K40 loops are colored red. (C, D) The structure of the α-K40 loop from PF B10. Red dashed boxes indicate the α-K40 loop. (E) Interaction of α-K40 loop of PF B10 with FAP52. FAP52’s K229 is within favorable distance to form hydrogen bonds with the backbone of D39 and T41. Hydrophobic interactions between L226 and I42 and interactions involving R225 are also possible.CC BY · PubMed Central
Figure 4—figure supplement 1. Data related to FAP52. (A) Atomic model of Chlamydomonas FAP52 from inside the Chlamydomonas density map. (B) Atomic model of Chlamydomonas FAP52 fitted inside the Tetrahymena map highlights the longer loop (red) from Chlamydomonas. (C) Alignment of FAP52 from several species shows that Chlamydomonas has a longer loop in one beta propeller blade. The long loop is responsible for the interaction with PACRG. (D, E) α-K40 loop from PF B9 in Chlamydomonas. (F, G) Superimposition of the acetylated α-K40 loops from Chlamydomonas PF B9, B10 and Tetrahymena A12.
Figure 4—figure supplement 1. Data related to FAP52. (A) Atomic model of Chlamydomonas FAP52 from inside the Chlamydomonas density map. (B) Atomic model of Chlamydomonas FAP52 fitted inside the Tetrahymena map highlights the longer loop (red) from Chlamydomonas. (C) Alignment of FAP52 from several species shows that Chlamydomonas has a longer loop in one beta propeller blade. The long loop is responsible for the interaction with PACRG. (D, E) α-K40 loop from PF B9 in Chlamydomonas. (F, G) Superimposition of the acetylated α-K40 loops from Chlamydomonas PF B9, B10 and Tetrahymena A12.CC BY · PubMed Central
Figure 5. Structure of the Tether densities. (A–B) At higher resolution, Tether densities 1 and 2 appear to be a single polypeptide chain in both Chlamydomonas (A) and Tetrahymena (B). Color scheme: tubulin: transparency gray; Tether densities 1 and 2 (Tether loop/FAP106): red; FAP276: purple; PACRG: light gray; Densities between PF A13 and A12 (turquoise). The dashed regions indicate the location of FAP52, which has been digitally removed to show the Tether densities underneath. (C) Model of FAP106 fitted inside the segmented Tether loop from Chlamydomonas. (D) Model of FAP106 tethering the B-tubule and A-tubule. Dashed box indicates view in (E). (E) Helix H3 and H4 of FAP106 insert into the gap formed by four tubulin dimers of PF B9 and B10. (F) Structure of Tether density 3 from Tetrahymena, which binds on top of the wedge between PF A13 and A1. (G) Overlay of the PACRG from Chlamydomonas onto the structure of Tetrahymena shows a hypothetical steric clash of a long Tetrahymena PACRG N-terminus with Tether density 3.
Figure 5. Structure of the Tether densities. (A–B) At higher resolution, Tether densities 1 and 2 appear to be a single polypeptide chain in both Chlamydomonas (A) and Tetrahymena (B). Color scheme: tubulin: transparency gray; Tether densities 1 and 2 (Tether loop/FAP106): red; FAP276: purple; PACRG: light gray; Densities between PF A13 and A12 (turquoise). The dashed regions indicate the location of FAP52, which has been digitally removed to show the Tether densities underneath. (C) Model of FAP106 fitted inside the segmented Tether loop from Chlamydomonas. (D) Model of FAP106 tethering the B-tubule and A-tubule. Dashed box indicates view in (E). (E) Helix H3 and H4 of FAP106 insert into the gap formed by four tubulin dimers of PF B9 and B10. (F) Structure of Tether density 3 from Tetrahymena, which binds on top of the wedge between PF A13 and A1. (G) Overlay of the PACRG from Chlamydomonas onto the structure of Tetrahymena shows a hypothetical steric clash of a long Tetrahymena PACRG N-terminus with Tether density 3.CC BY · PubMed Central
Figure 5—figure supplement 1. Data related to the Tether densities. (A) The density of the search motif [FHY]xWxxKxx[FHY used for identifying FAP106 (left panel) and the fitted model segment (right panel). (B) The model of the N-terminus (left) and C-terminus (right) of FAP106 inside the electron density. (C, D) The small helix (H2) (indicated by the dashed box) from Chlamydomonas (A) and Tetrahymena homolog for Tether loop appear to interact with α-tubulin. (E) Multiple sequence alignment of FAP106 from a few organisms. (F) Secondary structure prediction of FAP106. The big cylinder represents helical prediction. Low confidence predictions are omitted.
Figure 5—figure supplement 1. Data related to the Tether densities. (A) The density of the search motif [FHY]xWxxKxx[FHY used for identifying FAP106 (left panel) and the fitted model segment (right panel). (B) The model of the N-terminus (left) and C-terminus (right) of FAP106 inside the electron density. (C, D) The small helix (H2) (indicated by the dashed box) from Chlamydomonas (A) and Tetrahymena homolog for Tether loop appear to interact with α-tubulin. (E) Multiple sequence alignment of FAP106 from a few organisms. (F) Secondary structure prediction of FAP106. The big cylinder represents helical prediction. Low confidence predictions are omitted.CC BY · PubMed Central
Figure 6. Structure of FAP126 and its interaction. (A) View from the top of the PF A12 and A13 showing the density of FAP126 (dark turquoise). Dashed box indicates view in (B). (B) Closeup view of the interactions of FAP126 with the Tether loop, FAP106. T76 and Q77 of FAP126 form hydrogen bonds with Q126 and Q129 of FAP106, respectively. (C) Complimentary electrostatic surface charges of tubulins and FAP126. (D) Electrostatic charge of FAP126 on the tubulin interacting surface. (E) The N-terminus of PACRG and the hook density go into the wedges between PF A12 and A13, and PF A13 and A1, respectively. This likely contributes to the curvature of this region. (F) Inter-PF angles of the A- and B-tubules from Chlamydomonas and Tetrahymena (Ichikawa et al., 2019) showing very similar angle distributions. (G and H) Correlation graphs of consensus normalized expression levels for two selected pairs of genes (ENKURIN(FAP106)/FAP126 and FAP52/FAP126). Tissues showing high levels of expression of one or both genes are labeled. Correlation coefficients (r) are indicated. By excluding testis, corpus callosum, pons and medulla and fallopian tube, the correlation coefficients between ENKUR and FAP126 and between FAP52 and FAP126 are 0.66 and 0.84, respectively.
Figure 6. Structure of FAP126 and its interaction. (A) View from the top of the PF A12 and A13 showing the density of FAP126 (dark turquoise). Dashed box indicates view in (B). (B) Closeup view of the interactions of FAP126 with the Tether loop, FAP106. T76 and Q77 of FAP126 form hydrogen bonds with Q126 and Q129 of FAP106, respectively. (C) Complimentary electrostatic surface charges of tubulins and FAP126. (D) Electrostatic charge of FAP126 on the tubulin interacting surface. (E) The N-terminus of PACRG and the hook density go into the wedges between PF A12 and A13, and PF A13 and A1, respectively. This likely contributes to the curvature of this region. (F) Inter-PF angles of the A- and B-tubules from Chlamydomonas and Tetrahymena (Ichikawa et al., 2019) showing very similar angle distributions. (G and H) Correlation graphs of consensus normalized expression levels for two selected pairs of genes (ENKURIN(FAP106)/FAP126 and FAP52/FAP126). Tissues showing high levels of expression of one or both genes are labeled. Correlation coefficients (r) are indicated. By excluding testis, corpus callosum, pons and medulla and fallopian tube, the correlation coefficients between ENKUR and FAP126 and between FAP52 and FAP126 are 0.66 and 0.84, respectively.CC BY · PubMed Central
Figure 6—figure supplement 1. Data related to FAP126. (A) Multiple sequence alignment of FAP126 from a few organisms. FAP126 of Chlamydomonas still have the SH3 binding domain while lacks the proline-rich region compared to other species. (B) Atomic model of FAP126 fitted inside its segmented density. The dotted box indicated the view in (C). (C) The density of the search motif WPxxxxxW used for identifying FAP126. (D) Table of pairwise correlation coefficients between tissue mRNA expression levels, color-coded from low (red) to high (blue) values. ENKUR is the homolog of FAP106 in human. DCX is a microtubule associated protein in neuron, picked as a control. (E, F) Correlation graphs of consensus normalized expression levels for two selected pairs of genes (PACRG/FAP20 and PACRG/FAP52). Tissues showing high levels of expression of one or both genes are labeled. Correlation coefficients (r) are indicated.
Figure 6—figure supplement 1. Data related to FAP126. (A) Multiple sequence alignment of FAP126 from a few organisms. FAP126 of Chlamydomonas still have the SH3 binding domain while lacks the proline-rich region compared to other species. (B) Atomic model of FAP126 fitted inside its segmented density. The dotted box indicated the view in (C). (C) The density of the search motif WPxxxxxW used for identifying FAP126. (D) Table of pairwise correlation coefficients between tissue mRNA expression levels, color-coded from low (red) to high (blue) values. ENKUR is the homolog of FAP106 in human. DCX is a microtubule associated protein in neuron, picked as a control. (E, F) Correlation graphs of consensus normalized expression levels for two selected pairs of genes (PACRG/FAP20 and PACRG/FAP52). Tissues showing high levels of expression of one or both genes are labeled. Correlation coefficients (r) are indicated.CC BY · PubMed Central
Figure 7. Inner junction structure and proposed model of IJ formation. (A) Model of the IJ complex including PACRG, FAP20, FAP52, FAP126, FAP276 and FAP106. FAP45 is not depicted here. Tubulin is depicted as transparent. (B) The B-tubule starts growing laterally from the outer junction side as shown in Schmidt-Cernohorska et al. (2019). PACRG and FAP20 form a heterodimer, which binds onto the outside surface of PF A1. Following this, multiple alternative hypotheses are possible. One hypothesis is that FAP52, FAP276 and FAP106 would bind onto PF A12 and A13. FAP45 and other fMIP proteins would then be incorporated inside the B-tubule, which fixes the proper curvature so that PF B9 and B10 can interact with other IJ proteins. FAP52 binds both PF B9 and B10 through their K40 loops and finally, PACRG and FAP20 interact with the lateral side of PF B10 allowing for B-tubule closure.
Figure 7. Inner junction structure and proposed model of IJ formation. (A) Model of the IJ complex including PACRG, FAP20, FAP52, FAP126, FAP276 and FAP106. FAP45 is not depicted here. Tubulin is depicted as transparent. (B) The B-tubule starts growing laterally from the outer junction side as shown in Schmidt-Cernohorska et al. (2019). PACRG and FAP20 form a heterodimer, which binds onto the outside surface of PF A1. Following this, multiple alternative hypotheses are possible. One hypothesis is that FAP52, FAP276 and FAP106 would bind onto PF A12 and A13. FAP45 and other fMIP proteins would then be incorporated inside the B-tubule, which fixes the proper curvature so that PF B9 and B10 can interact with other IJ proteins. FAP52 binds both PF B9 and B10 through their K40 loops and finally, PACRG and FAP20 interact with the lateral side of PF B10 allowing for B-tubule closure.CC BY · PubMed Central

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Authors
Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., Bechstedt, S., Trempe, J.-F., & Bui, K. H.
Affiliations
  • McGill University (CA)
  • Kyoto University (JP)
Corresponding author
Bui, Khanh Huy
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2020-01-17
Volume
9
ISSN
2050-084X (ISSN-L)
DOI
10.7554/elife.52760
PMC
PMC6994238
OpenAlex
W3000377151
Cited by
1,676
References
67
Citations by year
2026: 159 · 2025: 264 · 2024: 275 · 2023: 301 · 2022: 336 · 2021: 273 · 2020: 64
FWCI
142.78
Type
journal article
Language
en
Open access
Licence
Locations
  • eLife (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Canadian Institutes of Health Research (PJT-156354)
  • Natural Sciences and Engineering Research Council of Canada (RGPIN-2016-04954, RGPIN-2018-04813, RGPIN-2017-04649)
  • Canadian Institute for Advanced Research (Arzieli Global Scholar Program)
  • Japan Society for the Promotion of Science
  • Abdulla Al Ghurair Foundation for Education (Al Ghurair STEM program scholarship)
  • Canada Research Chairs (950-229792)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Cystic Fibrosis Research Advances
Keywords
tubulin post-translational modifications, Chlamydomonas reinhardtii, Tetrahymena thermophila, ciliary motility, microtubule stability, cryo-electron microscopy
MeSH terms
Cilia, Microtubules, Plant Proteins, Protein Processing, Post-Translational, Mass Spectrometry, Protozoan Proteins, Tetrahymena thermophila, Chlamydomonas reinhardtii, Computational Biology, Cryoelectron Microscopy

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