title: A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption.
abstract: Mammalian oocytes are arrested at prophase I of meiosis, and resume meiosis prior to ovulation. Coordination of meiotic arrest and resumption is partly dependent on the post-transcriptional regulation of maternal transcripts. Here, we report that, SPINDLIN1 (SPIN1), a maternal protein containing Tudor-like domains, interacts with a known mRNA-binding protein SERBP1, and is involved in regulating maternal transcripts to control meiotic resumption. Mouse oocytes deficient for Spin1 undergo normal folliculogenesis, but are defective in resuming meiosis. SPIN1, via its Tudor-like domain, forms a ribonucleoprotein complex with SERBP1, and regulating mRNA stability and/or translation. The mRNA for the cAMP-degrading enzyme, PDE3A, is reduced in Spin1 mutant oocytes, possibly contributing to meiotic arrest. Our study demonstrates that Spin1 regulates maternal transcripts post-transcriptionally and is involved in meiotic resumption.
authors.affiliation: Mammalian Development Laboratory, Institute of Medical Biology, A-STAR, Singapore, Singapore. tinggang80@gmail.com
authors.forename: Ting Gang
authors.initials: TG
authors.lastname: Chew
authors.forename: Anne
authors.initials: A
authors.lastname: Peaston
authors.forename: Ai Khim
authors.initials: AK
authors.lastname: Lim
authors.forename: Chanchao
authors.initials: C
authors.lastname: Lorthongpanich
authors.forename: Barbara B
authors.initials: BB
authors.lastname: Knowles
authors.forename: Davor
authors.initials: D
authors.lastname: Solter
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005260:Female; D005786:Gene Expression Regulation; D006820:Hyaluronic Acid / Q000378:metabolism; D008297:Male; D008540:Meiosis; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009035:Mothers; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D018006:Myogenic Regulatory Factors / Q000378:metabolism; D009865:Oocytes / Q000166:cytology* / Q000378:metabolism; D006080:Ovarian Follicle / Q000254:growth & development; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism*
chemical_list: D018797:Cell Cycle Proteins; D008869:Microtubule-Associated Proteins; D018006:Myogenic Regulatory Factors; D010750:Phosphoproteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; C532831:SERBP1 protein, mouse; C104434:spindlin; D006820:Hyaluronic Acid
references.citation: Reproduction. 2011 Jun;141(6):737-47
references.pmid: 21411693
references.citation: J Cell Biochem. 2012 Aug;113(8):2721-8
references.pmid: 22442049
references.citation: Mol Biol Cell. 2005 Sep;16(9):4124-38
references.pmid: 15975911
references.citation: J Biol Chem. 2001 Feb 2;276(5):3341-7
references.pmid: 11001948
references.citation: Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):12011-6
references.pmid: 17620599
references.citation: Gene. 2008 Feb 29;410(1):67-74
references.pmid: 18201843
references.citation: Mol Hum Reprod. 2010 Sep;16(9):654-64
references.pmid: 20453035
references.citation: J Cell Physiol. 2008 Nov;217(2):400-8
references.pmid: 18543248
references.citation: Science. 2004 Dec 10;306(5703):1947-50
references.pmid: 15591206
references.citation: FEBS Lett. 2011 Aug 19;585(16):2556-60
references.pmid: 21771594
references.citation: Mol Biol Int. 2011;2011:163827
references.pmid: 22091396
references.citation: Development. 2009 Jun;136(11):1869-78
references.pmid: 19429786
references.citation: Nat Rev Mol Cell Biol. 2011 Sep 14;12(10):629-42
references.pmid: 21915143
references.citation: EMBO J. 1994 Dec 1;13(23):5712-20
references.pmid: 7988567
references.citation: Science. 2010 Oct 15;330(6002):366-9
references.pmid: 20947764
references.citation: Biol Reprod. 1996 Dec;55(6):1427-36
references.pmid: 8949903
references.citation: EMBO J. 1996 May 15;15(10):2582-92
references.pmid: 8665866
references.citation: FEBS J. 2006 Sep;273(17):3946-61
references.pmid: 16879614
references.citation: Development. 2000 Sep;127(17):3795-803
references.pmid: 10934024
references.citation: Cell. 2010 Oct 29;143(3):470-84
references.pmid: 21029866
references.citation: Reproduction. 2006 Jul;132(1):21-31
references.pmid: 16816330
references.citation: Curr Biol. 2010 Aug 24;20(16):R666-7
references.pmid: 20728048
references.citation: Mol Endocrinol. 2002 Feb;16(2):331-41
references.pmid: 11818504
references.citation: Annu Rev Physiol. 2007;69:483-510
references.pmid: 17305471
references.citation: Development. 1997 Jan;124(2):493-503
references.pmid: 9053325
references.citation: EMBO Rep. 2011 Oct 28;12(11):1160-6
references.pmid: 21960006
references.citation: J Cell Biol. 1974 Feb;60(2):416-22
references.pmid: 4813213
references.citation: Hum Reprod. 2010 Apr;25(4):957-68
references.pmid: 20147335
references.citation: Reproduction. 2005 Dec;130(6):791-9
references.pmid: 16322539
references.citation: Biochem Soc Trans. 2008 Aug;36(Pt 4):671-6
references.pmid: 18631138
references.citation: Dev Biol. 2012 Jun 15;366(2):308-16
references.pmid: 22546688
references.citation: Development. 2011 Sep;138(17):3735-44
references.pmid: 21795279
references.citation: Cell. 2009 Feb 6;136(3):496-507
references.pmid: 19167051
references.citation: Dev Biol. 2000 May 1;221(1):1-9
references.pmid: 10772787
references.citation: Nat Struct Biol. 2001 Jan;8(1):27-31
references.pmid: 11135666
references.citation: Trends Cell Biol. 2010 Aug;20(8):482-90
references.pmid: 20541937
references.citation: Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17639-44
references.pmid: 20876089
references.citation: J Biol Chem. 2007 Jan 5;282(1):647-56
references.pmid: 17082182