Testis-specific serine/threonine protein kinase 4 (Tssk4) phosphorylates Odf2 at Ser-76

Xiaoli Wang1, Han Li1,2, Guolong Fu3

  • 1Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, School of Pharmaceutical Sciences, and Medical Research Institute, Wuhan University, Wuhan, 430072, P.R.China.

Scientific Reports
|March 11, 2016
PubMed

Insights

Testis-specific serine/threonine protein kinase 4 (Tssk4) phosphorylates Odf2 at serine 76. This finding provides crucial insights into Tssk4

Area of Science:

  • Reproductive Biology
  • Molecular Cell Biology
  • Biochemistry

Background:

  • Tssk4 is a testis-specific kinase crucial for male fertility.
  • Tssk4 associates with and phosphorylates Odf2, but the specific site was unknown.

Purpose of the Study:

  • To identify the specific phosphorylation site on Odf2 targeted by Tssk4.
  • To elucidate the functional implications of Tssk4-mediated Odf2 phosphorylation in male fertility.

Main Methods:

  • Site-directed mutagenesis of Odf2 to generate point mutants (Ser/Thr/Lys to Ala).
  • Confirmation of Tssk4-Odf2 interaction domain (C-terminal region, amino acids 214-638).
  • In vivo analysis of phosphorylated Odf2 in mouse sperm using phospho-specific antibodies and LC-MS/MS.

Main Results:

  • The C-terminal region of Odf2 (amino acids 214-638) is necessary for Tssk4 association.
  • Serine 76 of Odf2 was identified as a key phosphorylation site by Tssk4.
  • Phosphorylated Odf2 was detected in mouse sperm, confirming in vivo relevance.

Conclusions:

  • This study identifies Serine 76 as a Tssk4 phosphorylation site on Odf2.
  • These findings offer critical insights into Tssk4's role in regulating sperm function and male fertility.

Related Concept Videos

Phosphorylation01:02

Phosphorylation

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...
55.5K
Phosphorylation01:02

Phosphorylation

7.9K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.5K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.7K
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
10.9K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
6.2K