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PMID:18202122

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Citation

Jha, KN, Shumilin, IA, Digilio, LC, Chertihin, O, Zheng, H, Schmitz, G, Visconti, PE, Flickinger, CJ, Minor, W and Herr, JC (2008) Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation. Endocrinology 149:2108-20

Abstract

The physiological changes that sperm undergo in the female reproductive tract rendering them fertilization-competent constitute the phenomenon of capacitation. Cholesterol efflux from the sperm surface and protein kinase A (PKA)-dependent phosphorylation play major regulatory roles in capacitation, but the link between these two phenomena is unknown. We report that apolipoprotein A-I binding protein (AI-BP) is phosphorylated downstream to PKA activation, localizes to both sperm head and tail domains, and is released from the sperm into the media during in vitro capacitation. AI-BP interacts with apolipoprotein A-I, the component of high-density lipoprotein involved in cholesterol transport. The crystal structure demonstrates that the subunit of the AI-BP homodimer has a Rossmann-like fold. The protein surface has a large two compartment cavity lined with conserved residues. This cavity is likely to constitute an active site, suggesting that AI-BP functions as an enzyme. The presence of AI-BP in sperm, its phosphorylation by PKA, and its release during capacitation suggest that AI-BP plays an important role in capacitation possibly providing a link between protein phosphorylation and cholesterol efflux.

Links

PubMed PMC2329272 Online version:10.1210/en.2007-0582

Keywords

Amino Acid Sequence; Animals; Antibodies/isolation & purification; Antibodies/metabolism; Apolipoprotein A-I/metabolism; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism; Carrier Proteins/physiology; Cholesterol/metabolism; Cloning, Molecular; Crystallography, X-Ray; Cyclic AMP-Dependent Protein Kinases/metabolism; DNA, Complementary/isolation & purification; Escherichia coli; Guinea Pigs; Male; Mice; Models, Molecular; Molecular Sequence Data; Phosphoproteins/chemistry; Phosphoproteins/genetics; Phosphoproteins/isolation & purification; Phosphoproteins/metabolism; Phosphoproteins/physiology; Phosphorylation; Sequence Homology, Amino Acid; Sperm Capacitation/genetics; Spermatozoa/metabolism; Tissue Distribution

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:KAPCA

acts_upstream_of_or_within

GO:0006468: protein phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:KAPCA

enables

GO:0004672: protein kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

  • has_input:(MGI:MGI:2180167)

Seeded From UniProt

complete

MOUSE:NNRE

located_in

GO:0005615: extracellular space

ECO:0000314: direct assay evidence used in manual assertion

C

  • adjacent_to:(CL:0000019)

Seeded From UniProt

complete

MOUSE:NNRE

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

PR:Q8K4Z3

F

Seeded From UniProt

complete

MOUSE:NNRE

located_in

GO:0005929: cilium

ECO:0000314: direct assay evidence used in manual assertion

C

  • part_of:(CL:0000019)

Seeded From UniProt

complete

MOUSE:NNRE

located_in

GO:0044297: cell body

ECO:0000314: direct assay evidence used in manual assertion

C

  • part_of:(CL:0000019)

Seeded From UniProt

complete

MOUSE:KAPCA

acts_upstream_of_or_within

GO:0006468: protein phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

has_participant:(MGI:MGI:2180167)

Seeded From UniProt

complete

MOUSE:KAPCA

enables

GO:0004672: protein kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

has_direct_input:(MGI:MGI:2180167)

Seeded From UniProt

complete


See also

References

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