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Article: Dynein 1 supports spermatid transport and spermiation during spermatogenesis in the rat testis

TitleDynein 1 supports spermatid transport and spermiation during spermatogenesis in the rat testis
Authors
KeywordsActin
Dynein 1
Ectoplasmic specialization
Microtubule
Spermatogenesis
Testis
Issue Date2018
PublisherAmerican Physiological Society. The Journal's web site is located at http://ajpendo.physiology.org/
Citation
American Journal of Physiology: Endocrinology and Metabolism, 2018, v. 315 n. 5, p. E924-E948 How to Cite?
AbstractIn the mammalian testis, spermatogenesis is dependent on the microtubule (MT)-specific motor proteins, such as dynein 1, that serve as the engine to support germ cell and organelle transport across the seminiferous epithelium at different stages of the epithelial cycle. Yet the underlying molecular mechanism(s) that support this series of cellular events remain unknown. Herein, we used RNAi to knockdown cytoplasmic dynein 1 heavy chain (Dync1h1) and an inhibitor ciliobrevin D to inactivate dynein in Sertoli cells in vitro and the testis in vivo, thereby probing the role of dynein 1 in spermatogenesis. Both treatments were shown to extensively induce disruption of MT organization across Sertoli cells in vitro and the testis in vivo. These changes also perturbed the transport of spermatids and other organelles (such as phagosomes) across the epithelium. These changes thus led to disruption of spermatogenesis. Interestingly, the knockdown of dynein 1 or its inactivation by ciliobrevin D also perturbed gross disruption of F-actin across the Sertoli cells in vitro and the seminiferous epithelium in vivo, illustrating there are cross talks between the two cytoskeletons in the testis. In summary, these findings confirm the role of cytoplasmic dynein 1 to support the transport of spermatids and organelles across the seminiferous epithelium during the epithelial cycle of spermatogenesis.
Persistent Identifierhttp://hdl.handle.net/10722/262488
ISSN
2021 Impact Factor: 5.900
2020 SCImago Journal Rankings: 1.507
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWen, Q-
dc.contributor.authorTang, EIY-
dc.contributor.authorLui, WY-
dc.contributor.authorLee, WWM-
dc.contributor.authorWong, CKC-
dc.contributor.authorSilvestrini, B-
dc.contributor.authorCheng, CY-
dc.date.accessioned2018-09-28T05:00:08Z-
dc.date.available2018-09-28T05:00:08Z-
dc.date.issued2018-
dc.identifier.citationAmerican Journal of Physiology: Endocrinology and Metabolism, 2018, v. 315 n. 5, p. E924-E948-
dc.identifier.issn0193-1849-
dc.identifier.urihttp://hdl.handle.net/10722/262488-
dc.description.abstractIn the mammalian testis, spermatogenesis is dependent on the microtubule (MT)-specific motor proteins, such as dynein 1, that serve as the engine to support germ cell and organelle transport across the seminiferous epithelium at different stages of the epithelial cycle. Yet the underlying molecular mechanism(s) that support this series of cellular events remain unknown. Herein, we used RNAi to knockdown cytoplasmic dynein 1 heavy chain (Dync1h1) and an inhibitor ciliobrevin D to inactivate dynein in Sertoli cells in vitro and the testis in vivo, thereby probing the role of dynein 1 in spermatogenesis. Both treatments were shown to extensively induce disruption of MT organization across Sertoli cells in vitro and the testis in vivo. These changes also perturbed the transport of spermatids and other organelles (such as phagosomes) across the epithelium. These changes thus led to disruption of spermatogenesis. Interestingly, the knockdown of dynein 1 or its inactivation by ciliobrevin D also perturbed gross disruption of F-actin across the Sertoli cells in vitro and the seminiferous epithelium in vivo, illustrating there are cross talks between the two cytoskeletons in the testis. In summary, these findings confirm the role of cytoplasmic dynein 1 to support the transport of spermatids and organelles across the seminiferous epithelium during the epithelial cycle of spermatogenesis.-
dc.languageeng-
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://ajpendo.physiology.org/-
dc.relation.ispartofAmerican Journal of Physiology: Endocrinology and Metabolism-
dc.subjectActin-
dc.subjectDynein 1-
dc.subjectEctoplasmic specialization-
dc.subjectMicrotubule-
dc.subjectSpermatogenesis-
dc.subjectTestis-
dc.titleDynein 1 supports spermatid transport and spermiation during spermatogenesis in the rat testis-
dc.typeArticle-
dc.identifier.emailWen, Q: wenqing8@HKUCC-COM.hku.hk-
dc.identifier.emailLui, WY: wylui@hku.hk-
dc.identifier.emailLee, WWM: hrszlwm@hku.hk-
dc.identifier.emailCheng, CY: cheng@popcbr.rockefeller.edu-
dc.identifier.authorityLui, WY=rp00756-
dc.identifier.authorityLee, WWM=rp00728-
dc.identifier.doi10.1152/ajpendo.00114.2018-
dc.identifier.pmid30016153-
dc.identifier.scopuseid_2-s2.0-85056574732-
dc.identifier.hkuros292332-
dc.identifier.volume315-
dc.identifier.issue5-
dc.identifier.spageE924-
dc.identifier.epageE948-
dc.identifier.isiWOS:000451048700017-
dc.publisher.placeUnited States-
dc.identifier.issnl0193-1849-

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