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Article: Zyxin, Axin, and Wiskott-Aldrich Syndrome Protein Are Adaptors That Link the Cadherin/Catenin Protein Complex to the Cytoskeleton at Adherens Junctions in the Seminiferous Epithelium of the Rat Testis

TitleZyxin, Axin, and Wiskott-Aldrich Syndrome Protein Are Adaptors That Link the Cadherin/Catenin Protein Complex to the Cytoskeleton at Adherens Junctions in the Seminiferous Epithelium of the Rat Testis
Authors
KeywordsAdaptors
Sertoli cells
Testis
Issue Date2004
PublisherAmerican Society of Andrology. The Journal's web site is located at http://www.andrologyjournal.org
Citation
Journal Of Andrology, 2004, v. 25 n. 2, p. 200-215 How to Cite?
AbstractDuring spermatogenesis, the movement of germ cells across the seminiferous epithelium is associated with extensive junction restructuring. Yet the underlying mechanism (or mechanisms) that regulates these events is largely unknown. If the molecular architecture of the cell-cell actin-based adherens junction (AJ), such as ectoplasmic specialization (ES) and tubulobulbar complex-two testis-specific AJ types, is known, many functional mechanistic studies can be designed. We thus undertook an investigation to study 3 adaptors in the seminiferous epithelium: zyxin, axin, and Wiskott-Aldrich syndrome protein (WASP). All 3 adaptors were shown to be products of Sertoli and germ cells. Zyxin was shown to be a stage-specific protein that was most prominent during stages V-VII and restricted mostly to pachytene spermatocytes, but it could also be detected at the site of basal and apical ectoplasmic specialization (ES). Zyxin, axin, and WASP were shown to be structurally linked to the N-cadherin/β-catenin/α-actinin/actin complex but not to the nectin-3/afadin or the β1-integrin-mediated protein complexes. Interestingly, zyxin, axin, and WASP are also structurally linked to vimentin (an intermediate filament protein) and α-tubulin (the subunit of a microtubule), which suggests that they have a role (or roles) in the regulation of the dynamics of the desmosome-like junction and microtubule. These results illustrate that zyxin, axin, and WASP are adaptors in both AJs and intermediate filament-based desmosome-like junctions. This raises the possibility that classic cadherins are also associated with vimentin-based intermediate filaments via these adaptors in the testis. While virtually no N-cadherin was found to associate with vimentin in the seminiferous tubules, it did associate with vimentin when testis lysates were used. Interestingly, about 5% of the E-cadherin associated with vimentin in isolated seminiferous tubules, and about 50% of the E-cadherin in the testis used vimentin as its attachment site. These data suggest that cadherins in the testis, unlike those in other epithelia, use different attachment sites to anchor the cadherin/catenin complex to the cytoskeleton. The levels of zyxin, axin, and WASP were also assessed during AF-2364-mediated AJ disruption of the testis, which illustrated a time-dependent protein reduction that was similar to the trends observed in nectin-3 and afadin but was the opposite of those observed for N-cadherin and β-catenin, which were induced. Collectively, these results illustrate that while these adaptors are structurally associated with the cadherin/catenin complex in the testis, they are regulated differently.
Persistent Identifierhttp://hdl.handle.net/10722/143470
ISSN
2014 Impact Factor: 2.473
2015 SCImago Journal Rankings: 0.867
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorConway, AMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2011-12-02T05:19:12Z-
dc.date.available2011-12-02T05:19:12Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Andrology, 2004, v. 25 n. 2, p. 200-215en_HK
dc.identifier.issn0196-3635en_HK
dc.identifier.urihttp://hdl.handle.net/10722/143470-
dc.description.abstractDuring spermatogenesis, the movement of germ cells across the seminiferous epithelium is associated with extensive junction restructuring. Yet the underlying mechanism (or mechanisms) that regulates these events is largely unknown. If the molecular architecture of the cell-cell actin-based adherens junction (AJ), such as ectoplasmic specialization (ES) and tubulobulbar complex-two testis-specific AJ types, is known, many functional mechanistic studies can be designed. We thus undertook an investigation to study 3 adaptors in the seminiferous epithelium: zyxin, axin, and Wiskott-Aldrich syndrome protein (WASP). All 3 adaptors were shown to be products of Sertoli and germ cells. Zyxin was shown to be a stage-specific protein that was most prominent during stages V-VII and restricted mostly to pachytene spermatocytes, but it could also be detected at the site of basal and apical ectoplasmic specialization (ES). Zyxin, axin, and WASP were shown to be structurally linked to the N-cadherin/β-catenin/α-actinin/actin complex but not to the nectin-3/afadin or the β1-integrin-mediated protein complexes. Interestingly, zyxin, axin, and WASP are also structurally linked to vimentin (an intermediate filament protein) and α-tubulin (the subunit of a microtubule), which suggests that they have a role (or roles) in the regulation of the dynamics of the desmosome-like junction and microtubule. These results illustrate that zyxin, axin, and WASP are adaptors in both AJs and intermediate filament-based desmosome-like junctions. This raises the possibility that classic cadherins are also associated with vimentin-based intermediate filaments via these adaptors in the testis. While virtually no N-cadherin was found to associate with vimentin in the seminiferous tubules, it did associate with vimentin when testis lysates were used. Interestingly, about 5% of the E-cadherin associated with vimentin in isolated seminiferous tubules, and about 50% of the E-cadherin in the testis used vimentin as its attachment site. These data suggest that cadherins in the testis, unlike those in other epithelia, use different attachment sites to anchor the cadherin/catenin complex to the cytoskeleton. The levels of zyxin, axin, and WASP were also assessed during AF-2364-mediated AJ disruption of the testis, which illustrated a time-dependent protein reduction that was similar to the trends observed in nectin-3 and afadin but was the opposite of those observed for N-cadherin and β-catenin, which were induced. Collectively, these results illustrate that while these adaptors are structurally associated with the cadherin/catenin complex in the testis, they are regulated differently.en_HK
dc.languageengen_US
dc.publisherAmerican Society of Andrology. The Journal's web site is located at http://www.andrologyjournal.orgen_HK
dc.relation.ispartofJournal of Andrologyen_HK
dc.subjectAdaptorsen_HK
dc.subjectSertoli cellsen_HK
dc.subjectTestisen_HK
dc.subject.meshAdherens Junctionsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCadherinsen_US
dc.subject.meshCarrier Proteinsen_US
dc.subject.meshCells - Cultureden_US
dc.subject.meshCytoskeletal Proteinsen_US
dc.subject.meshCytoskeletonen_US
dc.subject.meshElectrophoresis - Polyacrylamide Gelen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshIntracellular Signaling Peptides and Proteinsen_US
dc.subject.meshMaleen_US
dc.subject.meshMicroscopy - Electronen_US
dc.subject.meshMicroscopy - Fluorescenceen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshRatsen_US
dc.subject.meshRats - Sprague - Dawleyen_US
dc.subject.meshRepressor Proteinsen_US
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen_US
dc.subject.meshSeminiferous Epitheliumen_US
dc.subject.meshSertoli Cellsen_US
dc.subject.meshSpermatozoaen_US
dc.subject.meshTrans - Activatorsen_US
dc.subject.meshbeta Cateninen_US
dc.titleZyxin, Axin, and Wiskott-Aldrich Syndrome Protein Are Adaptors That Link the Cadherin/Catenin Protein Complex to the Cytoskeleton at Adherens Junctions in the Seminiferous Epithelium of the Rat Testisen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid14760006-
dc.identifier.scopuseid_2-s2.0-1242342879en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1242342879&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume25en_HK
dc.identifier.issue2en_HK
dc.identifier.spage200en_HK
dc.identifier.epage215en_HK
dc.identifier.isiWOS:000189382200010-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridConway, AM=36862532100en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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