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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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The journey of sperm from its origin to the point of ejaculation begins within the seminiferous tubules of the testis. Here, Sertoli cells produce fluid that propels non-motile sperm through a series of conduits, starting with the straight tubules leading to the rete testis. This interconnected network of tubules acts as the initial pathway for sperm, guiding them into the efferent ductules and then into the epididymis for maturation.
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During ejaculation, males release around 2-5 milliliters of semen, which is a complex mixture of mature sperm and various fluids produced by accessory glands. The mature sperm cells measure approximately 60 micrometers in length and consist of a head, neck, midpiece, and tail. The head is flattened and tapered, measuring about 4 to 5 micrometers in length. It contains a nucleus with condensed chromosomes and an acrosome, a cap-like structure filled with enzymes essential for penetrating the...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Using an Extracellular Flux Analyzer to Measure Changes in Glycolysis and Oxidative Phosphorylation during Mouse Sperm Capacitation
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Serine/threonine phosphorylation associated with hamster sperm hyperactivation.

Masakatsu Fujinoki1, Tadashi Ishimoda-Takagi1, Hideki Ohtake1

  • 1Department of Physiology, Dokkyo University School of Medicine, Mibu, Tochigi and Department of Biology, Tokyo Gakugei University, Koganei, Tokyo, Japan.

Reproductive Medicine and Biology
|April 18, 2018
PubMed
Summary
This summary is machine-generated.

Mammalian sperm hyperactivation involves serine and threonine phosphorylation, not just tyrosine. A 10-kDa protein is dual-phosphorylated during this process, suggesting complex regulation of sperm function.

Keywords:
dephosphorylationhamstershyperactivationphosphorylationspermatozoa

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Area of Science:

  • Reproductive Biology
  • Molecular Endocrinology
  • Sperm Physiology

Background:

  • Sperm activation and hyperactivation are crucial for mammalian fertilization.
  • Protein phosphorylation, particularly tyrosine phosphorylation, plays a key regulatory role.
  • The involvement of serine and threonine phosphorylation in these processes requires further investigation.

Purpose of the Study:

  • To investigate the role of serine and threonine phosphorylation in mammalian sperm activation and hyperactivation.
  • To identify specific proteins involved in these phosphorylation events.

Main Methods:

  • Western blotting using antiphospho-amino acid monoclonal antibodies to detect protein phosphorylation in hamster spermatozoa.
  • Tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein separation.
  • Peptide sequencing to analyze amino acid sequences of phosphorylated proteins.

Main Results:

  • Four proteins (90, 38, 32, and 10 kDa) were phosphorylated at serine residues during hyperactivation.
  • Five proteins (90, 70, 65, 35, and 10 kDa) were phosphorylated or dephosphorylated at threonine residues.
  • A 10-kDa protein, previously identified as a tyrosine phosphoprotein, showed similarity to carcinustatin.

Conclusions:

  • Sperm hyperactivation involves significant serine phosphorylation and threonine phospho- or dephosphorylation events.
  • The 10-kDa protein undergoes tyrosine phosphorylation during activation and subsequent serine and threonine phosphorylation during hyperactivation.
  • These findings highlight the complex, multi-site phosphorylation patterns regulating sperm function.