A novel ankyrin‐repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of <i>Chlamydomonas reinhardtii</i>

Ikeda, Kazuho; Yamamoto, Ryōichi; Wirschell, Maureen; Yagi, Toshiki; Bower, Raqual; Porter, Mary E.; Sale, Winfield S.; Kamiya, Ritsu

doi:10.1002/cm.20324

Cited by 36 publications

(51 citation statements)

References 42 publications

(48 reference statements)

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“…The observed mass differences between the I1 complex in bop5-1 and WT were three-to fivefold larger than expected based on previous biochemical studies (31,32), whereas the differences between bop5-1 and bop5-2 were surprisingly small. This suggested that the proteomic deficiencies in the bop5 mutants had not been fully characterized, making the interpretation of our structural data difficult.…”

Section: I1 Intermediate Chain Assembly Into the Axoneme Of Wt And I1contrasting

confidence: 66%

“…S7). FAP120 was previously detected as a single, relatively unfocused spot (32). Here, we resolved FAP120 into two spots, indicating a previously unknown posttranslational modification (Fig.…”

Section: I1 Intermediate Chain Assembly Into the Axoneme Of Wt And I1supporting

confidence: 51%

“…Comparison Between WT and bop5 Mutants Reveals the Location of the IC138 Subcomplex. The bop5-1 mutant has a point mutation in the IC138 gene that results in a truncated IC138 polypeptide and defective assembly of the ICLC, lacking FAP120 and LC7b (31,32). According to our cryo-ET structure, the mass of the bop5-1 ICLC is ∼40% reduced compared with WT (Fig.…”

Section: Resultsmentioning

confidence: 89%

“…6). Bop5-1 was previously thought to be missing only the C-terminal 8% of IC138, LC7b, and FAP120 (2-3 copies per I1), that is, roughly a difference of 110-150 kDa compared with WT (31,32). It was therefore surprising that our bop5-1 averages suggested a loss of ∼500 kDa compared with WT ( Fig.…”

Section: Internal Architecture Of the I1 Complex And Localization Of I1mentioning

confidence: 79%

“…1). A number of I1 components have been identified biochemically, including three intermediate chains (IC140, IC138, and IC97), several light chains (LC8, LC7a, LC7b, Tctex1, and Tctex2b), and the accessory protein FAP120 (11,13,16,(23)(24)(25)(28)(29)(30)(31)(32)(33)(34). A recent study of an IC138 null mutant (bop5-2) revealed that IC138 is required for assembly of an "IC138 subcomplex" consisting of IC138, IC97, LC7b, and FAP120 (21).…”

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confidence: 99%

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Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein

Heuser

Barber

Lin

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Cilia and flagella are highly conserved motile and sensory organelles in eukaryotes, and defects in ciliary assembly and motility cause many ciliopathies. The two-headed I1 inner arm dynein is a critical regulator of ciliary and flagellar beating. To understand I1 architecture and function better, we analyzed the 3D structure and composition of the I1 dynein in Chlamydomonas axonemes by cryoelectron tomography and subtomogram averaging. Our data revealed several connections from the I1 dynein to neighboring structures that are likely to be important for assembly and/or regulation, including a tether linking one I1 motor domain to the doublet microtubule and doublet-specific differences potentially contributing to the asymmetrical distribution of dynein activity required for ciliary beating. We also imaged three I1 mutants and analyzed their polypeptide composition using 2D gel-based proteomics. Structural and biochemical comparisons revealed the likely location of the regulatory IC138 phosphoprotein and its associated subcomplex. Overall, our studies demonstrate that I1 dynein is connected to multiple structures within the axoneme, and therefore ideally positioned to integrate signals that regulate ciliary motility.dynein f | flagella C ilia and flagella are highly conserved organelles with roles in cellular movement and signal transduction. In humans, defects in cilia can lead to a number of diseases, such as polycystic kidney disease and primary ciliary dyskinesia (1, 2). The axoneme core of most motile cilia and flagella consists of nine doublet microtubules (DMTs) surrounding two single microtubules (MTs) known as the central pair complex (CPC) (Fig. 1). DMTs are highly periodic with a 96-nm-long unit that repeats along the MT length. They are decorated with two rows of dynein motors, the inner dynein arms (IDAs) and the outer dynein arms (ODAs), which drive MT sliding and axoneme bending (3). Generating the diverse ciliary and flagellar waveforms requires the precise coordination of the activity of thousands of dynein motors within a single organelle (4).The primary signaling pathway known to regulate dynein function in axonemes involves signals traveling from the CPC through radial spokes (RSs) to the IDAs and ODAs (reviewed in 5, 6). Many CPC and RS mutants are paralyzed (7). However, MT sliding can be restored to WT levels in isolated CPC/RS mutant axonemes using protein kinase inhibitors (8, 9). These observations, together with biochemical evidence of phosphorylation of dynein subunits, have implicated the dyneins as a major signaling target of the CPC/RS signaling pathway (10, 11). However, the regulatory mechanisms and physical interactions that participate in signal transduction to the dynein targets are not well understood.Isolated axonemes require only ATP for reactivation, suggesting that direct interactions between the dyneins and their regulators are physically built into the axoneme (4). Therefore, studies that visualize axonemal structures and their connections at high resolution can provide ...

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Section: I1 Intermediate Chain Assembly Into the Axoneme Of Wt And I1contrasting

confidence: 66%

Section: I1 Intermediate Chain Assembly Into the Axoneme Of Wt And I1supporting

confidence: 51%

Section: Resultsmentioning

confidence: 89%

Section: Internal Architecture Of the I1 Complex And Localization Of I1mentioning

confidence: 79%

mentioning

confidence: 99%

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Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein

Heuser

Barber

Lin

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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133

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Proteopedia entry: Citrate synthase

Decatur¹,

Eddelman²

2011

Biochem Molecular Bio Educ

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Background: A large number of studies have shown that psychological treatments have significant effects on depression. Although several studies have examined the relative effects of psychological and combined treatments, this has not been studied satisfactorily in recent statistical meta‐analyses. Method: We conducted a meta‐analysis of randomized studies in which a psychological treatment was compared to a combined treatment consisting of the same psychological treatment with a pharmacological therapy. For each of these studies we calculated the effect size indicating the difference between the psychological and the combined treatment. Results: All inclusion criteria were met by 18 studies, with a total of 1,838 subjects. The mean effect size indicating the difference between psychological and combined treatment was 0.35 (95% CI: 0.24∼0.45; P<0.001), with low heterogeneity. Subgroup analyses indicated that the difference between psychological and combined treatments was significantly smaller in studies in which cognitive behavior therapy was examined. We also found a trend (P<0.1) indicating that the difference between psychological and combined treatment was somewhat larger in studies aimed at specific populations (older adults, chronic depression, HIV patients) than in studies with adults, and in studies in which Trycyclic antidepressants or SSRIs were examined, compared to studies in which a medication protocol or another antidepressant was used. At follow‐up, no difference between psychological and combined treatments was found. Conclusion: We conclude that combined treatment is more effective than psychological treatment alone. However, it is not clear whether this difference is relevant from a clinical perspective. Depression and Anxiety, 2009. © 2008 Wiley‐Liss, Inc.

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An axonemal PP2A B‐subunit is required for PP2A localization and flagellar motility

et al. 2011

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Analysis of Chlamydomonas axonemes revealed that the protein phosphatase, PP2A, is localized to the outer doublet microtubules and is implicated in regulation of dynein-driven motility. We tested the hypothesis that PP2A is localized to the axoneme by a specialized, highly conserved 55-kDa B-type subunit identified in the Chlamydomonas flagellar proteome. The B-subunit gene is defective in the motility mutant pf4. Consistent with our hypothesis, both the B- and C-subunits of PP2A fail to assemble in pf4 axonemes, while the dyneins and other axonemal structures are fully assembled in pf4 axonemes. Two pf4 intragenic revertants were recovered that restore PP2A to the axonemes and re-establish nearly wild-type motility. The revertants confirmed that the slow-swimming Pf4 phenotype is a result of the defective PP2A B-subunit. These results demonstrate that the axonemal B-subunit is, in part, an anchor protein required for PP2A localization and that PP2A is required for normal ciliary motility.

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A novel ankyrin‐repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii

Cited by 36 publications

References 42 publications

Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein

Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein

Proteopedia entry: Citrate synthase

An axonemal PP2A B‐subunit is required for PP2A localization and flagellar motility

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