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Article: 14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesis

Title14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesis
Authors
Issue Date2009
PublisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
Citation
Journal Of Endocrinology, 2009, v. 202 n. 3, p. 327-336 How to Cite?
AbstractDuring spermatogenesis, spermiation takes place at the adluminal edge of the seminiferous epithelium at stage VIII of the epithelial cycle during which fully developed spermatids (i.e. spermatozoa) detach from the epithelium in adult rat testes. This event coincides with the migration of preleptotene/leptotene spermatocytes across the blood-testis barrier from the basal to the apical (or adluminal) compartment. At stage XIV of the epithelial cycle, Pachytene spermatocytes (diploid, 2n) differentiate into diplotene spermatocytes (tetraploid, 4n) in the apical compartment of the epithelium, which begin meiosis I to be followed by meiosis II to form spermatids (haploid, 1n) at stage XIV of the epithelial cycle. These spermatids, in turn, undergo extensive morphological changes and traverse the seminiferous epithelium until they differentiate into elongated spermatids. Thus, there are extensive changes at the Sertoli-Sertoli and Sertoli-germ cell interface via protein 'coupling' and 'uncoupling' between cell adhesion protein complexes, as well as changes in interactions between integral membrane proteins and their peripheral adaptors, regulatory protein kinases and phosphatases, and the cytoskeletal proteins. These precisely coordinated protein-protein interactions affect cell adhesion and cell movement. In this review, we focus on the 14-3-3 protein family, whose members have different binding partners in the seminiferous epithelium. Recent studies have illustrated that 14-3-3 affects protein-protein interactions in the seminiferous epithelium, and regulates cell adhesion possibly via its effects on intracellular protein trafficking and cell-polarity proteins. This review provides a summary on the latest findings regarding the role of 14-3-3 family of proteins and their potential implications on spermatogenesis. We also highlight research areas that deserve attentions by investigators. © 2009 Society for Endocrinology.
Persistent Identifierhttp://hdl.handle.net/10722/179160
ISSN
2015 Impact Factor: 4.498
2015 SCImago Journal Rankings: 1.910
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Sen_US
dc.contributor.authorWong, EWPen_US
dc.contributor.authorLi, MWMen_US
dc.contributor.authorLee, WMen_US
dc.contributor.authorCheng, CYen_US
dc.date.accessioned2012-12-19T09:52:27Z-
dc.date.available2012-12-19T09:52:27Z-
dc.date.issued2009en_US
dc.identifier.citationJournal Of Endocrinology, 2009, v. 202 n. 3, p. 327-336en_US
dc.identifier.issn0022-0795en_US
dc.identifier.urihttp://hdl.handle.net/10722/179160-
dc.description.abstractDuring spermatogenesis, spermiation takes place at the adluminal edge of the seminiferous epithelium at stage VIII of the epithelial cycle during which fully developed spermatids (i.e. spermatozoa) detach from the epithelium in adult rat testes. This event coincides with the migration of preleptotene/leptotene spermatocytes across the blood-testis barrier from the basal to the apical (or adluminal) compartment. At stage XIV of the epithelial cycle, Pachytene spermatocytes (diploid, 2n) differentiate into diplotene spermatocytes (tetraploid, 4n) in the apical compartment of the epithelium, which begin meiosis I to be followed by meiosis II to form spermatids (haploid, 1n) at stage XIV of the epithelial cycle. These spermatids, in turn, undergo extensive morphological changes and traverse the seminiferous epithelium until they differentiate into elongated spermatids. Thus, there are extensive changes at the Sertoli-Sertoli and Sertoli-germ cell interface via protein 'coupling' and 'uncoupling' between cell adhesion protein complexes, as well as changes in interactions between integral membrane proteins and their peripheral adaptors, regulatory protein kinases and phosphatases, and the cytoskeletal proteins. These precisely coordinated protein-protein interactions affect cell adhesion and cell movement. In this review, we focus on the 14-3-3 protein family, whose members have different binding partners in the seminiferous epithelium. Recent studies have illustrated that 14-3-3 affects protein-protein interactions in the seminiferous epithelium, and regulates cell adhesion possibly via its effects on intracellular protein trafficking and cell-polarity proteins. This review provides a summary on the latest findings regarding the role of 14-3-3 family of proteins and their potential implications on spermatogenesis. We also highlight research areas that deserve attentions by investigators. © 2009 Society for Endocrinology.en_US
dc.languageengen_US
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.orgen_US
dc.relation.ispartofJournal of Endocrinologyen_US
dc.rightsJournal of Endocrinology. Copyright © Society for Endocrinology.-
dc.title14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesisen_US
dc.typeArticleen_US
dc.identifier.emailLee, WM: hrszlwm@hku.hken_US
dc.identifier.authorityLee, WM=rp00728en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1677/JOE-09-0041en_US
dc.identifier.pmid19366886-
dc.identifier.scopuseid_2-s2.0-70349317276en_US
dc.identifier.hkuros164874-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70349317276&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume202en_US
dc.identifier.issue3en_US
dc.identifier.spage327en_US
dc.identifier.epage336en_US
dc.identifier.isiWOS:000272629900001-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridSun, S=34977782600en_US
dc.identifier.scopusauthoridWong, EWP=23029194700en_US
dc.identifier.scopusauthoridLi, MWM=27168276300en_US
dc.identifier.scopusauthoridLee, WM=24799156600en_US
dc.identifier.scopusauthoridCheng, CY=7404797787en_US

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