期刊论文详细信息
Developmental Biology
CABYR, a Novel Calcium-Binding Tyrosine Phosphorylation-Regulated Fibrous Sheath Protein Involved in Capacitation
Arabinda Mandal1  John C. Herr1  V.Anne Westbrook1  Soren Naaby-Hansen1  Young-Howan Kim1  Leigh Ann Bush1  Buer Sen1  Scott A. Coonrod1  Charles J. Flickinger1  Michael J. Wolkowicz1  Jagathpala Shetty1  Kenneth L. Klotz1 
[1] Ludwig Institute for Cancer Research, Royal Free and University College School of Medicine, London, W1P 8BT, United Kingdom
关键词: CABYR;    spermatozoa;    capacitation;    calcium-binding protein;    fibrous sheath;    tyrosine phosphorylation;    postmeiotic expression;   
DOI  :  10.1006/dbio.2001.0527
学科分类:生物科学(综合)
来源: Academic Press
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【 摘 要 】

Toreachfertilizationcompetence,spermundergoanincompletelyunderstoodseriesofmorphologicalandmolecularmaturationalprocesses,termedcapacitation,involving,amongotherprocesses,proteintyrosinephosphorylationandincreasedintracellularcalcium.Hyperactivatedmotilityandanabilitytoundergotheacrosomereactionserveasphysiologicalendpointstoassesssuccessfulcapacitation.Wereportherethatacidic(pI4.0)86-kDaisoformsofanovel,polymorphic,testis-specificprotein,designatedcalcium-bindingtyrosinephosphorylation-regulatedprotein(CABYR),weretyrosinephosphorylatedduringinvitrocapacitationandbound45Caon2Dgels.Acidic86-kDacalcium-bindingformsofCABYRincreasedduringinvitrocapacitation,andcalciumbindingtotheseacidicformswasabolishedbydephosphorylationwithalkalinephosphatase.SixvariantsofCABYRcontainingtwocodingregions(CR-AandCR-B)wereclonedfromhumantestiscDNAlibraries,includingfivevariantswithalternativesplicedeletions.AmotifhomologoustotheRIIdimerizationdomainofPK-AwaspresentintheN-terminusofCR-AinfourCABYRvariants.AsingleputativeEFhandlikemotifwasnotedinCR-Aataas197–209,whilesevenpotentialtyrosinephosphorylation-likesiteswerenotedinCR-AandfourinCR-B.Pro-X-X-Pro(PXXP)moduleswereidentifiedintheN-andC-terminiofCR-AandCR-B.CABYRlocalizestotheprincipalpieceofthehumanspermflagelluminassociationwiththefibroussheathandisthefirstdemonstrationofaspermproteinthatgainscalcium-bindingcapacitywhenphosphorylatedduringcapacitation.

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