Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida

Flesch, Frits M.; Wijnand, E.; Lest, Chris H.A. van de; Colenbrander, B.; Golde, L.M.G. Van; Gadella, Bart M.

doi:10.1002/mrd.1067

Cited by 52 publications

(28 citation statements)

References 44 publications

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“…Furthermore, the localization of phosphorylated proteins in the acrosome of capacitated sperm, together with its further loss after the acrosome reaction, could be related to the activation of certain proteins involved in this process (Dube et al 2005). Similarly, as reported in several mammalian species, zona pellucida binding induced phosphorylation in the midpiece (Leyton & Saling 1989, Flesch et al 2001) and other tail regions (Urner et al 2001.…”

Section: Discussionmentioning

confidence: 62%

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Grasa

Colás²,

Gallego³

et al. 2009

Reproduction

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Previously, we reported the involvement of tyrosine phosphorylation in events that lead to ram sperm capacitation. In this study, we carried out a comparative analysis of the localization of tyrosine, serine and threonine phosphoproteins in different functional stages of ram spermatozoa (after the swim-up procedure, in vitro capacitation, and ionophore-induced acrosome reaction) by immunofluorescence, immunocytochemistry and confocal microscopy. Capacitation increased protein tyrosine, serine and threonine phosphorylation whereas the induction of the acrosome reaction resulted in significantly decreased phosphorylation, mainly in those proteins that increased following capacitation. Control samples showed tyrosine-phosphorylated proteins restricted to the head, mainly distributed at the equatorial region with some cells also displaying an acrosomal and/or post-acrosomal localization. In vitro capacitation promoted both tail and acrosome phosphorylation, and the acrosome reaction induced the loss of labeling on the acrosome and the subsequent increase in the post-acrosomal region and flagellum. The preferential localization of serine-and threonine-phosphorylated proteins in the equatorial and acrosomal regions found in control samples changed during capacitation, which induced tail phosphorylation in a sequential manner. After the acrosome reaction, the labeling of both phosphoamino acids decreased in the acrosome and increased in the post-acrosome. The obtained results were proved by two immunodetection techniques and strengthened by confocal microscopy, and indicate that changes in phosphorylated proteins during capacitation and acrosome reaction of ram spermatozoa may have physiological significance in consolidating certain phosphorylated proteins to specific sperm regions involved in acrosomal exocytosis and zona pellucida recognition, binding and penetration. Reproduction (2009) 137 655-667

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Section: Discussionmentioning

confidence: 62%

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Grasa

Colás²,

Gallego³

et al. 2009

Reproduction

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“…2C). The possibility of a relationship between plasma membrane phosphoprotein expression and zona binding has been alluded to in other mammalian species (Flesch et al, 1999;Flesch et al, 2001;Tardif et al, 2001). However, this is the first report of the appearance of tyrosinephosphorylated proteins on the surface of live mouse spermatozoa during capacitation.…”

Section: Discussionmentioning

confidence: 94%

Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition

Asquith

Baleato

McLaughlin

et al. 2004

Journal of Cell Science

182

181

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Mammalian spermatozoa undergo a series of molecular and biochemical changes collectively termed capacitation prior to acquiring the ability to fertilise the oocyte. Although phosphorylation of sperm proteins on tyrosine residues has been recognised as an important component of this process, the precise relationship between the phosphorylation status of mammalian spermatozoa and their capacity for fertilisation has remained unclear. In this study we demonstrate a causal relationship between tyrosine phosphorylation in spermatozoa and sperm-zona interaction. The phosphotyrosine expression associated with sperm capacitation localised to internal flagellar structures in permeabilised cells but could also be detected on the exterior surface of the sperm head in live cells. Importantly, almost all spermatozoa bound to the zona pellucida demonstrated this pattern of phosphoprotein localisation, compared to fewer than 15% of the free-swimming population. These data suggest that tyrosine phosphorylation plays a significant role in remodelling the sperm surface, so that these cells are able to recognise the zona pellucida. Phosphoproteome analysis yielded the first evidence of molecular chaperones, endoplasmin (erp99) and heat shock protein 60 (hsp60), as targets for phosphorylation on the surface of mouse spermatozoa, whereas immunofluorescence localised these proteins to the precise region of the sperm head that participates in zona recognition. Based on these results, we propose a novel mechanism for mammalian gamete interaction whereby the activation of sperm-surface chaperones by tyrosine phosphorylation during capacitation may trigger conformational changes facilitating the formation of a functional zona pellucida receptor complex on the surface of mammalian spermatozoa.

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“…Some of these techniques, however, tend to give low purifications and poorly defined fractions, or involve treatments that denature proteins, inhibit enzyme activity, or affect the functional integrity of the membranes. Careful evaluation of the strategy is especially relevant for proteins involved in ZP recognition; if the preparation contains acrosomal contamination, intra-acrosomal ZP-binding proteins will be identified that may mask primary (plasma membrane) ZP-binding proteins (14). An alternative to subcellular fractionation is enrichment in protein types from a whole cell lysate.…”

mentioning

confidence: 99%

“…Alternatively, immobilized lectins are used in affinity chromatography to extract surface glycoproteins (18), a method that can also be employed on nitrogen-cavitated and solubilized sperm plasma membrane material. Finally, sperm head plasma membrane proteins with high primary ZP binding affinity have been specifically isolated using ZP fragment columns (14,19).…”

mentioning

confidence: 99%

Identification of Bovine Sperm Surface Proteins Involved in Carbohydrate-mediated Fertilization Interactions

Defaus

Sánchez

Andreu

et al. 2016

Molecular & Cellular Proteomics

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Glycan-protein interactions play a key role in mammalian fertilization, but data on the composition and identities of protein complexes involved in fertilization events are scarce, with the added complication that the glycans in such interactions tend to differ among species. In this study we have used a bovine model to detect, characterize and identify sperm lectins relevant in fertilization. Given the complexity of the sperm-toward-egg journey, two important aspects of the process, both primarily mediated by protein-sugar interactions, have been addressed: (1) formation of the sperm reservoir in the oviductal epithelium, and (2) gamete recognition (oocytesperm interaction). Using whole sperm cells and a novel affinity capture method, several groups of proteins with different glycan specificities, including 58 hitherto unreported as lectins, have been identified in sperm surface, underscoring both the efficacy of our selective approach and the complex composition and function of sperm. Based on these results and previous data, we suggest that sperm surface proteins play significant roles in fertilization events such as membrane remodeling, transport, protection and function, thus supporting the hypothesis that rather than a simple lock-and-key model, mammalian fertilization relies on a complex interactome involving multiple ligands/receptors and recognition/binding events. Molecular & Cellular

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Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida

Cited by 52 publications

References 44 publications

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition

Identification of Bovine Sperm Surface Proteins Involved in Carbohydrate-mediated Fertilization Interactions

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