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
2011 Impact Factor: 2.484
2011 SCImago Journal Rankings: 0.287
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 Field
Value
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
2011 Impact Factor: 2.484
2011 SCImago Journal Rankings: 0.287
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
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