Kinesin-5 Eg5 is essential for spindle assembly and chromosome alignment of mouse spermatocytes

She, Zhen‐Yu; Zhong, Ning; Yu, Kun; Xiao, Yu; Wei, Ya‐Lan; Yang, Lin; Li, Yueling; Lu, Ming‐Hui

doi:10.1186/s13008-020-00063-4

Cited by 14 publications

(6 citation statements)

References 67 publications

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“…When a specific/selective KIF11 inhibitor such as Monastrol, S-trityl- l -cysteine, or Dimethylenastron was injected into mouse testis, dividing spermatocytes exhibited impaired spindle bipolarity following KIF11 suppression. KIF11 inhibition also causes a reduction in spermatid count and defective sperm in mice ( She et al, 2020a ). By immunofluorescent staining, KIF10 from kinesin-7 family was revealed to be expressed in germ cells in the mouse testis.…”

Section: Kinesins In Germ Cell Development In Mammalian Testesmentioning

confidence: 99%

“…As in the case of KIF11, it remains to be verified whether it is restricted to germ cells (esp. spermatogonia and spermatocytes) rather than somatic Sertoli cells of the mouse testis ( Hara-Yokoyama et al, 2019 ; She et al, 2020a ), e.g., by immunoblotting and/or mRNA analysis utilizing purified germ or Sertoli cells isolated from rodent testes.…”

Section: Kinesins In Germ Cell Development In Mammalian Testesmentioning

confidence: 99%

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Kinesins in Mammalian Spermatogenesis and Germ Cell Transport

Yao

Han

et al. 2022

Front. Cell Dev. Biol.

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In mammalian testes, the apical cytoplasm of each Sertoli cell holds up to several dozens of germ cells, especially spermatids that are transported up and down the seminiferous epithelium. The blood-testis barrier (BTB) established by neighboring Sertoli cells in the basal compartment restructures on a regular basis to allow preleptotene/leptotene spermatocytes to pass through. The timely transfer of germ cells and other cellular organelles such as residual bodies, phagosomes, and lysosomes across the epithelium to facilitate spermatogenesis is important and requires the microtubule-based cytoskeleton in Sertoli cells. Kinesins, a superfamily of the microtubule-dependent motor proteins, are abundantly and preferentially expressed in the testis, but their functions are poorly understood. This review summarizes recent findings on kinesins in mammalian spermatogenesis, highlighting their potential role in germ cell traversing through the BTB and the remodeling of Sertoli cell-spermatid junctions to advance spermatid transport. The possibility of kinesins acting as a mediator and/or synchronizer for cell cycle progression, germ cell transit, and junctional rearrangement and turnover is also discussed. We mostly cover findings in rodents, but we also make special remarks regarding humans. We anticipate that this information will provide a framework for future research in the field.

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Section: Kinesins In Germ Cell Development In Mammalian Testesmentioning

confidence: 99%

Section: Kinesins In Germ Cell Development In Mammalian Testesmentioning

confidence: 99%

Kinesins in Mammalian Spermatogenesis and Germ Cell Transport

Yao

Han

et al. 2022

Front. Cell Dev. Biol.

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“…Vertebrate Eg5 is a homotetrameric motor that has two pairs of motor domains (also called heads) at opposite ends of a central stalk. Each pair of heads can bind to one MT and move processively toward the plus end of MT by hydrolyzing ATP molecules. − Eg5 motors slide apart antiparallel MTs and are critical to anaphase MT motions. − Nonmotor MAP PRC1 exists in human cells and is a member of the conserved family of MAP. Individual members in this family have different names from different species, including homologues Ase1 (in budding yeast), MAP65 (in plants), and Feo (in flies and worms). , PRC1 has two MT-binding domains (also called heads) located at two ends of the central stalk.…”

Section: Introductionmentioning

confidence: 99%

Computational Studies Reveal How Passive Cross-Linkers Regulate Anaphase Spindle Elongation

Wang,

Liu,

Wang

et al. 2024

J. Phys. Chem. B

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In eukaryotic cell division, a series of events are organized to produce two daughter cells. The spindle elongation in anaphase B is essential for providing enough space to maintain cell size and distribute sister chromatids properly, which is associated with microtubules and microtubule-associated proteins such as kinesin-5 Eg5 and the Ase1related protein, PRC1. The available experimental data indicated that after the start of anaphase B more PRC1 proteins can bind to the antiparallel microtubule pairs in the spindle but the excess amount of PRC1 proteins can lead to the failure of cell division, indicating that PRC1 proteins can regulate the spindle elongation in a concentrationdependent manner. However, the underlying mechanism of the PRC1 proteins regulating the spindle elongation has not been explained up to now. Here, we use a simplified model, where only the two important participants (kinesin-5 Eg5 motors and PRC1 proteins) are considered, to study the spindle elongation during anaphase B. We first show that only in the appropriate range of the PRC1 concentration can the spindle elongation complete properly. Furthermore, we explore the underlying mechanism of PRC1 as a regulator for spindle elongation.

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“…They can either stabilize or destabilize microtubule plus ends. One such interesting candidate is kinesin-5, also known as Eg5 or KIF11, which is essential for bipolar spindle assembly and regulation of spindle elongation (Saunders et al, 2007;Brust-Mascher et al, 2009;She et al, 2020;Pandey et al, 2021). It is a homotetrameric motor protein that can crosslink microtubules and slide them against each other by walking in both directions (Kapitein et al, 2005;Scholey et al, 2014).…”

Section: Microtubule Plus-end Regulationmentioning

confidence: 99%

Dynamic life of a microtubule

Rai¹

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Microtubules are one of the major types of cytoskeletal filaments in cells. They are very dynamic polymers composed of αβ-tubulin dimers arranged longitudinally in head-to-tail fashion as well as laterally to assemble 13-protofilament hollow cylindrical tubes. The incorporation of GTP-bound αβ-tubulin dimers generates a fast growing plus end exposing β-tubulin and a slow growing minus end exposing α-tubulin. In cells, microtubules are assembled de novo from a template, called γ-TuRC, which interacts with α-tubulin. Microtubules can either remain capped by γ-TuRC and anchored to the microtubule-organizing centers (MTOCs) or be released if they are cut by microtubule severing enzymes like katanin. The release of microtubules from MTOC generates free minus ends, which are then stabilized by minus-end binding proteins called CAMSAPs. However, the plus ends remain very dynamic and undergo transitions from growth to shrinkage, termed “catastrophes”, and the opposite transitions termed “rescues”. Numerous microtubule regulatory proteins act at the plus ends, minus ends and the microtubule shafts connecting the two ends to control the organization and density of cellular microtubule networks. In this thesis, we focused on each of these aspects and explored the dynamic life of microtubules by reconstituting these processes in vitro using purified proteins. We first focused on the birth and growth of microtubules. We reconstituted microtubule nucleation using purified γ-TuRC and microtubule regulatory proteins and showed that CDK5RAP2, CLASP2 and chTOG promoted microtubule nucleation from γ-TuRC. We discovered that CAMSAPs can bind to γ-TuRC-capped microtubule minus ends and displace γ-TuRC from these ends, generating free and stable microtubule minus ends. Furthermore, we found out that CDK5RAP2, but not CLASP2 or chTOG, can inhibit CAMSAP binding and microtubule release. We propose that the destiny of a microtubule depends on the type of protein complex that activates its nucleation. We then described a mechanism for stabilization of microtubule lattice by TRIM46, a neuronal protein, which can bundle parallel microtubules and promote microtubule rescues within these bundles. We also revealed that Ankyrin-G, a scaffold protein, can recruit TRIM46-stabilized microtubule bundles to the axonal membrane to drive the assembly of the axon initial segment in neurons. We also uncovered a new role of CLASP2 as a microtubule repair factor participating in microtubule maintenance. We demonstrated that CLASP2, an anti-catastrophe factor, can promote complete repair of damaged microtubule lattices by inhibiting microtubule depolymerization and promoting tube closure at the damage sites, causing lattice renewal. Finally, we described a three-protein module involving katanin, CAMSAPs, and WDR47 that can regulate microtubule polymer mass and minus-end stability. We showed that katanin can cut and amplify CAMSAP2/3-stabilized microtubule minus ends. WDR47 can inhibit the binding of katanin to CAMSAP2/3-stabilized minus ends and protect them from severing. The presence of WDR47 shifts the balance from microtubule amplification to minus-end growth regulation. To conclude, we obtained mechanistic insights into the regulation of microtubule nucleation, minus-end dynamics, lattice stabilization and maintenance, microtubule number and the interplay between microtubule regulatory proteins. These insights will help to understand how microtubule arrays are organized in cells.

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Kinesin-5 Eg5 is essential for spindle assembly and chromosome alignment of mouse spermatocytes

Cited by 14 publications

References 67 publications

Kinesins in Mammalian Spermatogenesis and Germ Cell Transport

Kinesins in Mammalian Spermatogenesis and Germ Cell Transport

Computational Studies Reveal How Passive Cross-Linkers Regulate Anaphase Spindle Elongation

Dynamic life of a microtubule

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