Structural specializations of the sperm tail

Leung, Miguel Ricardo; Zeng, Jianwei; Wang, Xiangli; Roelofs, Marc C.; Huang, Wei; Chiozzi, Riccardo Zenezini; Hevler, Johannes F.; Heck, Albert J. R.; Dutcher, Susan K.; Brown, Alan; Zhang, Rui; Zeev‐Ben‐Mordehai, Tzviya

doi:10.1016/j.cell.2023.05.026

Cited by 33 publications

(30 citation statements)

References 117 publications

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“…Most MIPs so far were found in axonemes with over 60 MIPs being revealed in sperm axonemes ( 7, 18 ). To investigate if there are MIPs in Plasmodium axonemes we searched for orthologs to known MIPs from other organisms using PlasmoDB.…”

Section: Resultsmentioning

confidence: 99%

“…Recently, an increasing number of proteins have been found that bind to the microtubule lattice from the inside of the microtubule and have been termed luminal or microtubule inner proteins (MIPs) ( 1–15 ). Nearly all MIPs have been initially identified in axonemes, including in sperm of metazoans and sea urchins or in flagella of protozoans ( 3, 11, 12, 15–18 ). Furthermore, several dozen of MIPs have been described in Chlamydomonas, Tetrahymena and sperm with mammalian sperm exhibiting the largest number of MIPs discovered so far ( 14, 15, 18 ).…”

Section: Introductionmentioning

confidence: 99%

“…Nearly all MIPs have been initially identified in axonemes, including in sperm of metazoans and sea urchins or in flagella of protozoans ( 3, 11, 12, 15–18 ). Furthermore, several dozen of MIPs have been described in Chlamydomonas, Tetrahymena and sperm with mammalian sperm exhibiting the largest number of MIPs discovered so far ( 14, 15, 18 ). Deletion of some of these MIPs were shown to affect flagellar or ciliar beating pattern ( 3, 14, 15 ).…”

Section: Introductionmentioning

confidence: 99%

“…To allow for better visibility, not all MTs are shown. C) Close-up on spMTs with predicted localisation of SPM1 and TrxL1 (based on ( 21 )) and axonemal MTs with predicted localisation of FAP20 and FAP52 (based on ( 10, 14, 15, 18 )).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Microtubule inner proteins ofPlasmodiumare essential for transmission of malaria parasites

Hentzschel,

Binder,

Dorner

et al. 2023

Preprint

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Microtubule inner proteins, MIPs, are microtubule associated proteins that bind to tubulin from the luminal side. MIPs can be found in axonemes to stabilize flagellar beat or within cytoplasmic microtubules. Plasmodium spp. are the causative agents of malaria that feature different forms across a complex life cycle with both unique and divergent microtubule-based arrays. Here we investigate the role of four MIPs in a rodent malaria parasite for their role in transmission to and from the mosquito. We show by single and double gene deletions that SPM1 and TrxL1, MIPs associated with the subpellicular microtubules are dispensable for transmission from the vertebrate host to the mosquito and back. In contrast, FAP20 and FAP52, MIPs associated with the axonemes of gametes, are essential for transmission to mosquitoes but only if both genes are deleted. In the absence of both, FAP20 and FAP52 the B-tubule of the axoneme partly detaches from the A-tubule resulting in the deficiency of axonemal beating and hence gamete formation and egress. Our data suggest that a high level of redundancy ensures microtubule stability in the transmissive stages of Plasmodium, which is important for parasite transmission.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Microtubule inner proteins ofPlasmodiumare essential for transmission of malaria parasites

Hentzschel,

Binder,

Dorner

et al. 2023

Preprint

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show abstract

“…On the contrary, the recent high-resolution cryoelectron microscopy (cryo-EM) structures of axonemes [4][5][6][7] visualized the detailed structure of axonemal dyneins. However, not all structures are equally resolved: The structures that are close to the A-tubules (e.g., the tail, the linker, and the ATPase domain) are well-resolved in the cryo-EM maps.…”

mentioning

confidence: 99%

A quest to unravel the role of the stalk and microtubule‐binding domain of axonemal dyneins

Kikkawa

2023

FEBS Letters

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Structure challenges in the multivalency of Tau‐microtubule interactions

Nogales,

Kellogg

2023

Cytoskeleton

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Structural studies aiming to visualize the interaction of Tau with microtubules (MTs) face several challenges, the main concerning the fact that Tau has multiple MT‐interacting regions. In particular, the four (or three) pseudo‐repeats of Tau bind to identical elements along the MT lattice but do it through non‐identical residues. In addition, any given Tau molecule can use all its repeats or just one for its engagement with MTs. Finally, the binding of one Tau is not necessarily in register with respect to the next one. The mismatch in the MT and Tau repeats, therefore, challenges conventional modes of image analysis when visualizing these samples using cryo‐electron microscopy. This commentary is dedicated to those challenges and ways to circumvent them while aiming for an atomic description of the Tau‐tubulin interaction.

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Structural specializations of the sperm tail

Cited by 33 publications

References 117 publications

Microtubule inner proteins ofPlasmodiumare essential for transmission of malaria parasites

Microtubule inner proteins ofPlasmodiumare essential for transmission of malaria parasites

A quest to unravel the role of the stalk and microtubule‐binding domain of axonemal dyneins

Structure challenges in the multivalency of Tau‐microtubule interactions

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