LRGUK-1 Is Required for Basal Body and Manchette Function during Spermatogenesis and Male Fertility

Liu, Yan; DeBoer, Kathleen D.; Kretser, David Morritz de; O’Donnell, Liza; O’Connor, Anne E; Merriner, D. Jo; Okuda, Hidenobu; Whittle, Belinda; Jans, David A.; Efthymiadis, Athina; McLachlan, Robert I; Ormandy, Christopher J.; Goodnow, Christopher C.; Jamsai, Duangporn; O'Bryan, Moira K

doi:10.1371/journal.pgen.1005090

Cited by 63 publications

(58 citation statements)

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“…HOOK1 belongs to HOOK protein family, which is known to function as cargo-loading proteins onto microtubules for transport. The depletion of an interaction partner of another HOOK protein family member, HOOK2, also causes cylindrical head shaping (Liu et al 2015). The uncharacterized protein called leucine-rich repeats and guanylate kinase domain containing isoform 1 (LRGUK1) is transported via acrosome-acroplaxome-manchette-tail axis in a complex with HOOK2.…”

Section: R50 M S Lehti and A Sironenmentioning

confidence: 99%

“…The uncharacterized protein called leucine-rich repeats and guanylate kinase domain containing isoform 1 (LRGUK1) is transported via acrosome-acroplaxome-manchette-tail axis in a complex with HOOK2. LRGUK1 dysfunction caused disorganized and uneven distribution of manchette microtubules and lack of the sperm tail axoneme (Liu et al 2015). The involvement of HOOK2/LRGUK1 complex has been suggested in protein transport, but the exact mechanism is not known.…”

Section: R50 M S Lehti and A Sironenmentioning

confidence: 99%

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Formation and function of the manchette and flagellum during spermatogenesis

Lehti¹,

Sironen²

2016

Reproduction

214

179

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The last phase of spermatogenesis involves spermatid elongation (spermiogenesis), where the nucleus is remodeled by chromatin condensation, the excess cytoplasm is removed and the acrosome and sperm tail are formed. Protein transport during spermatid elongation is required for correct formation of the sperm tail and acrosome and shaping of the head. Two microtubular-based protein delivery platforms transport proteins to the developing head and tail: the manchette and the sperm tail axoneme. The manchette is a transient skirt-like structure surrounding the elongating spermatid head and is only present during spermatid elongation. In this review, we consider current understanding of the assembly, disassembly and function of the manchette and the roles of these processes in spermatid head shaping and sperm tail formation. Recent studies have shown that at least some of the structural proteins of the sperm tail are transported through the intra-manchette transport to the basal body at the base of the developing sperm tail and through the intraflagellar transport to the construction site in the flagellum. This review focuses on the microtubule-based mechanisms involved and the consequences of their disruption in spermatid elongation.Reproduction (2016) 151 R43-R54

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Section: R50 M S Lehti and A Sironenmentioning

confidence: 99%

Section: R50 M S Lehti and A Sironenmentioning

confidence: 99%

Formation and function of the manchette and flagellum during spermatogenesis

Lehti¹,

Sironen²

2016

Reproduction

214

179

View full text Add to dashboard Cite

show abstract

“…63, 64 Sun4 -deficient mice lack the linkers between the nuclear envelope and the microtubule manchette. 65, 66 Azi1 -null spermatids show defective manchette structure and abnormal head morphologies, suggesting defects in intramanchette transport.…”

Section: Manchette Of Elongating Spermatidsmentioning

confidence: 99%

The control of male fertility by spermatid-specific factors: searching for contraceptive targets from spermatozoon’s head to tail

et al. 2016

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Male infertility due to abnormal spermatozoa has been reported in both animals and humans, but its pathogenic causes, including genetic abnormalities, remain largely unknown. On the other hand, contraceptive options for men are limited, and a specific, reversible and safe method of male contraception has been a long-standing quest in medicine. Some progress has recently been made in exploring the effects of spermatid-specifical genetic factors in controlling male fertility. A comprehensive search of PubMed for articles and reviews published in English before July 2016 was carried out using the search terms ‘spermiogenesis failure', ‘globozoospermia', ‘spermatid-specific', ‘acrosome', ‘infertile', ‘manchette', ‘sperm connecting piece', ‘sperm annulus', ‘sperm ADAMs', ‘flagellar abnormalities', ‘sperm motility loss', ‘sperm ion exchanger' and ‘contraceptive targets'. Importantly, we have opted to focus on articles regarding spermatid-specific factors. Genetic studies to define the structure and physiology of sperm have shown that spermatozoa appear to be one of the most promising contraceptive targets. Here we summarize how these spermatid-specific factors regulate spermiogenesis and categorize them according to their localization and function from spermatid head to tail (e.g., acrosome, manchette, head-tail conjunction, annulus, principal piece of tail). In addition, we emphatically introduce small-molecule contraceptives, such as BRDT and PPP3CC/PPP3R2, which are currently being developed to target spermatogenic-specific proteins. We suggest that blocking the differentiation of haploid germ cells, which rarely affects early spermatogenic cell types and the testicular microenvironment, is a better choice than spermatogenic-specific proteins. The studies described here provide valuable information regarding the genetic and molecular defects causing male mouse infertility to improve our understanding of the importance of spermatid-specific factors in controlling fertility. Although a male contraceptive ‘pill' is still many years away, research into the production of new small-molecule contraceptives targeting spermatid-specific proteins is the right avenue.

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“…By now, the delicate mechanism of human spermiogenesis and the genetic defects of DDS have not yet been explained completely 5. One of the major findings is the involvement of ‘manchette’ in the transformation of sperm tails and the nuclear condensation,6 which provides the microtubule track for protein transportation and facilitates the dynamic redistribution of the actin cytoskeletal system 7…”

Section: Introductionmentioning

confidence: 99%