PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility
Open accessAbstract
We previously demonstrated that PACRG plays a role in regulating dynein-driven microtubule sliding in motile cilia. To expand our understanding of the role of PACRG in ciliary assembly and motility, we used a combination of functional and structural studies, including newly identified Chlamydomonas pacrg mutants. Using cryo-electron tomography we show that PACRG and FAP20 form the inner junction between the A- and B-tubule along the length of all nine ciliary doublet microtubules. The lack of PACRG and FAP20 also results in reduced assembly of inner-arm dynein IDA b and the beak-MIP structures. In addition, our functional studies reveal that loss of PACRG and/or FAP20 causes severe cell motility defects and reduced in vitro microtubule sliding velocities. Interestingly, the addition of exogenous PACRG and/or FAP20 protein to isolated mutant axonemes restores microtubule sliding velocities, but not ciliary beating. Taken together, these studies show that PACRG and FAP20 comprise the inner junction bridge that serves as a hub for both directly modulating dynein-driven microtubule sliding, as well as for the assembly of additional ciliary components that play essential roles in generating coordinated ciliary beating.
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Disruption of the Chlamydomonas CFAP20 orthologue FAP20 alone does not break the B-to-A tubule connection.
“Notably, disruption of the Chlamydomonas CFAP20 orthologue (FAP20) alone does not break the B-to-A tubule connection20.”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
The Results section (Table 3; page not provided) reports B-to-A tubule detachment in the pacrg; fap20 double mutant, and the paper also studies a fap20 single mutant. It does not report whether the B-to-A connection remains intact in the fap20 single mutant, so the claim about FAP20 disruption alone is not directly established. (LLM, conf=0.75)
Experimental — accuracy not yet measuredIn Chlamydomonas or other unicellular eukaryotes, CFAP20, PACRG, CFAP45, CFAP52 and EFHC1/Rib72 are all needed to regulate ciliary beat patterns.
“Consistent with such a role, in Chlamydomonas or other unicellular eukaryotes, CFAP20, PACRG, CFAP45, CFAP52 and EFHC1/Rib72 are all needed to regulate ciliary beat patterns20,76–78.”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
The Results section reports that Chlamydomonas pacrg mutants cannot produce normal waveforms and that fap20 mutants have a similar motility defect. The Discussion mentions FAP52 and Rib72 in structural contexts, but does not establish that they regulate beat patterns; the cited passages also do not establish that role for CFAP45. Page numbers are not available in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredProteins at or near the inner junction, including CFAP20, PACRG, CFAP45, CFAP52, CFAP90, CFAP126 and EFHC1, are positioned to form a potential scaffold for, or functionally influence, the radial spokes and dynein regulatory complex that regulates ciliary motility.
“From cryo-EM structures of Chlamydomonas and Tetrahymena motile cilia, proteins at or near the inner junction, which include CFAP20, PACRG, CFAP45, CFAP52, CFAP90, CFAP126 and EFHC119–21, are all positioned to form a potential scaffold for, or functionally influence, the radial spokes and dynein regulatory complex that regulates ciliary motility (Fig. 8).”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
The Introduction and Discussion (page numbers unavailable) identify PACRG and FAP20 as inner-junction components and describe the junction as a potential hub for signals involving radial spokes and the nexin–dynein regulatory complex. This supports the proposed regulatory role for those two proteins, but the paper does not establish the listed roles of CFAP45, CFAP52, CFAP90, CFAP126, or EFHC1, nor does it report Tetrahymena structures. (LLM, conf=0.88)
Experimental — accuracy not yet measuredIn both C. elegans and Chlamydomonas, CFAP20 and PACRG localisation to the inner junction region is independent from each other.
“In both C. elegans and Chlamydomonas, CFAP20 and PACRG localisation to this region is independent from each other (Fig. S5b; ref. 20).”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
The Discussion (page not provided) says that PACRG and FAP20 can each assemble independently at the inner junction, based on Chlamydomonas mutant axonemes. The paper does not establish the same finding in C. elegans, so it supports only the Chlamydomonas part of the claim. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe inner junction is well positioned to act as a scaffold for the radial spoke and dynein regulatory complex machinery.
“Based on near-atomic-resolution cryo-electron microscopy reconstructions of motile cilia axonemes, the inner junction is well positioned to act as a scaffold for the radial spoke and dynein regulatory complex machinery19–22.”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
Recent studies position CFAP20 specifically as a core inner junction protein.
“Recent studies position CFAP20 specifically as a core inner junction protein16,19,20 (Fig. 1b).”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
There is a discontinuity in the CFAP20-PACRG arrangement at the inner junction, where a periodic absence of PACRG coincides with the association of the N-DRC with the axoneme.
“Remarkably, there is even a discontinuity in the CFAP20-PACRG arrangement at the inner junction, where a periodic absence of PACRG coincides with the association of the N-DRC (Nexin-Dynein Regulatory Complex) with the axoneme19,20.”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
The multiple contacts of CFAP20 with ciliary axoneme tubulins and PACRG, as well as proximity to CFAP52 and other proteins at or near the inner junction, could explain the degree of conservation of CFAP20.
“The multiple contacts of CFAP20 with ciliary axoneme tubulins and PACRG, as well as proximity to CFAP52 and other proteins at or near the inner junction19–21,71 (Figs. 1b and 8), could explain this degree of conservation.”
From The inner junction protein CFAP20 functions in motile and non-motile cilia and is critical for vision (2022) · cites this paper as [20]
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- Authors
- Dymek, E. E., Lin, J., Fu, G., Porter, M. E., Nicastro, D., & Smith, E. F.
- Affiliations
- Dartmouth College (US)
- The University of Texas Southwestern Medical Center (US)
- University of Minnesota (US)
- Corresponding author
- Smith, Elizabeth F.
- Venue
- Molecular Biology of the Cell
- Published
- 2019-07-15
- Volume
- 30
- Issue
- 15
- Pages
- 1805-1816
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC6727744
- OpenAlex
- W2946288900
- Cited by
- 61
- References
- 57
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 8 · 2023: 11 · 2022: 3 · 2021: 6 · 2020: 7 · 2019: 9
- FWCI
- 3.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Cancer Prevention and Research Institute of Texas (RP170644)
- University of Minnesota
- University of Texas Southwestern Medical Center
- National Institutes of Health (RP170644)
- National Institute of General Medical Sciences (R01GM055667, R01GM083122, R01GM112050)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Cystic Fibrosis Research Advances
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- PACRG, ciliary motility, inner dynein arm, Chlamydomonas, axoneme assembly, ciliary beating
- MeSH terms
- Cilia, Flagella, Microtubules, Movement, Mutation, Chlamydomonas reinhardtii, Algal Proteins, Axoneme
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