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Article: Male germ cell-specific protein Trs4 binds to multiple proteins
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TitleMale germ cell-specific protein Trs4 binds to multiple proteins
 
AuthorsShi, YQ2 3
Li, YC2
Hu, XQ2
Liu, T2
Liao, SY2
Guo, J2
Huang, L2
Hu, ZY2
Tang, AYB1
Lee, KF1
Yeung, WSB1
Han, CS2
Liu, YX2
 
KeywordsCryptorchidism
IQ calmodulin-binding motif
Spermatogenesis
Testis
Trs4
 
Issue Date2009
 
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
CitationBiochemical And Biophysical Research Communications, 2009, v. 388 n. 3, p. 583-588 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.bbrc.2009.08.053
 
AbstractTemperature-related sequence 4 (Trs4) has been identified as a testis-specific gene with expression sensitive to the abdominal temperature changes induced by artificial cryptorchidism. In murine testes, Trs4 mRNA was detected in round spermatids and its protein was localized mainly in the elongating spermatids as well as in the acrosomes and tails of mature spermatozoa. Using a yeast two-hybrid screening system, we identified Rshl-2, Gstmu1, and Ddc8 as putative binding partners of the Trs4 protein in mouse testes. Their interactions were confirmed by in vivo and in vitro binding assays. Further studies demonstrated that Ddc8, a newly identified gene with unknown functions, displayed a similar expression pattern with Trs4 in mouse testes. In particular, Trs4, Ddc8, and Rshl-2 proteins were co-localized to the tails of mature spermatozoa. These results suggested that Trs4 might be involved in diverse processes of spermiogenesis and/or fertilization through interactions with its multiple binding partners. © 2009 Elsevier Inc.
 
ISSN0006-291X
2013 Impact Factor: 2.281
 
DOIhttp://dx.doi.org/10.1016/j.bbrc.2009.08.053
 
ISI Accession Number IDWOS:000275061900022
Funding AgencyGrant Number
National Basic Research Program of China2006CB944000
2006CB944004
National "973" Program2006CB504001
NSFC-RGC30618005
N_HKU712/06
Beijing NSF5073032
CAS Knowledge Innovation ProjectKSCX2-YW-R-5
National Natural Science Foundation of China90508008
Funding Information:

This study was supported by the National Basic Research Program of China (2006CB944000, 2006CB944004), the National "973" Program (2006CB504001), the NSFC-RGC joint Project (30618005 and N_HKU712/06), Beijing NSF (5073032), the CAS Knowledge Innovation Project (KSCX2-YW-R-5) and the National Natural Science Foundation of China (90508008).

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorShi, YQ
 
dc.contributor.authorLi, YC
 
dc.contributor.authorHu, XQ
 
dc.contributor.authorLiu, T
 
dc.contributor.authorLiao, SY
 
dc.contributor.authorGuo, J
 
dc.contributor.authorHuang, L
 
dc.contributor.authorHu, ZY
 
dc.contributor.authorTang, AYB
 
dc.contributor.authorLee, KF
 
dc.contributor.authorYeung, WSB
 
dc.contributor.authorHan, CS
 
dc.contributor.authorLiu, YX
 
dc.date.accessioned2010-10-28T06:50:52Z
 
dc.date.available2010-10-28T06:50:52Z
 
dc.date.issued2009
 
dc.description.abstractTemperature-related sequence 4 (Trs4) has been identified as a testis-specific gene with expression sensitive to the abdominal temperature changes induced by artificial cryptorchidism. In murine testes, Trs4 mRNA was detected in round spermatids and its protein was localized mainly in the elongating spermatids as well as in the acrosomes and tails of mature spermatozoa. Using a yeast two-hybrid screening system, we identified Rshl-2, Gstmu1, and Ddc8 as putative binding partners of the Trs4 protein in mouse testes. Their interactions were confirmed by in vivo and in vitro binding assays. Further studies demonstrated that Ddc8, a newly identified gene with unknown functions, displayed a similar expression pattern with Trs4 in mouse testes. In particular, Trs4, Ddc8, and Rshl-2 proteins were co-localized to the tails of mature spermatozoa. These results suggested that Trs4 might be involved in diverse processes of spermiogenesis and/or fertilization through interactions with its multiple binding partners. © 2009 Elsevier Inc.
 
dc.description.naturepostprint
 
dc.identifier.citationBiochemical And Biophysical Research Communications, 2009, v. 388 n. 3, p. 583-588 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.bbrc.2009.08.053
 
dc.identifier.citeulike5442614
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.bbrc.2009.08.053
 
dc.identifier.epage588
 
dc.identifier.hkuros173151
 
dc.identifier.isiWOS:000275061900022
Funding AgencyGrant Number
National Basic Research Program of China2006CB944000
2006CB944004
National "973" Program2006CB504001
NSFC-RGC30618005
N_HKU712/06
Beijing NSF5073032
CAS Knowledge Innovation ProjectKSCX2-YW-R-5
National Natural Science Foundation of China90508008
Funding Information:

This study was supported by the National Basic Research Program of China (2006CB944000, 2006CB944004), the National "973" Program (2006CB504001), the NSFC-RGC joint Project (30618005 and N_HKU712/06), Beijing NSF (5073032), the CAS Knowledge Innovation Project (KSCX2-YW-R-5) and the National Natural Science Foundation of China (90508008).

 
dc.identifier.issn0006-291X
2013 Impact Factor: 2.281
 
dc.identifier.issue3
 
dc.identifier.openurl
 
dc.identifier.pmid19706271
 
dc.identifier.scopuseid_2-s2.0-69549138575
 
dc.identifier.spage583
 
dc.identifier.urihttp://hdl.handle.net/10722/124158
 
dc.identifier.volume388
 
dc.languageeng
 
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
dc.publisher.placeUnited States
 
dc.relation.ispartofBiochemical and Biophysical Research Communications
 
dc.relation.referencesReferences in Scopus
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subject.meshAmino Acid Sequence
 
dc.subject.meshCarrier Proteins - genetics - metabolism
 
dc.subject.meshSpermatogenesis
 
dc.subject.meshSpermatozoa - metabolism
 
dc.subject.meshTestis - metabolism
 
dc.subjectCryptorchidism
 
dc.subjectIQ calmodulin-binding motif
 
dc.subjectSpermatogenesis
 
dc.subjectTestis
 
dc.subjectTrs4
 
dc.titleMale germ cell-specific protein Trs4 binds to multiple proteins
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Institute of Zoology Chinese Academy of Sciences
  3. Weifang University