Related Experiment Video
Updated: Jun 12, 2026
11:11
Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
Published on: February 21, 2019
Protein kinase CK2 and new binding partners during spermatogenesis
Nadja Mannowetz1, Sabine Kartarius, Gunther Wennemuth
1Department of Anatomy and Cell Biology, University of the Saarland, Homburg, Germany.
Cellular and Molecular Life Sciences : CMLS
|June 5, 2010
Summary
Protein kinase CK2 subunits interact with TNP1 and KIF5C during sperm development. Their specific locations suggest roles in early and late spermatogenesis, impacting protein distribution in spermatozoa.
Area of Science:
- Cell Biology
- Molecular Biology
- Reproductive Biology
Background:
- Protein kinase CK2 (CK2) is vital for cell survival, existing as a holoenzyme or individual subunits.
- CK2 subunits interact with various cellular proteins, influencing diverse cellular processes.
Purpose of the Study:
- To investigate the expression and interaction of CK2 subunits (CK2α, CK2α', CK2β) during spermatogenesis.
- To identify novel binding partners of CK2 subunits during sperm development.
- To determine the localization of CK2 subunits and their interacting proteins in mature spermatozoa.
Main Methods:
- Immunohistochemistry to detect protein expression and localization.
- Co-immunoprecipitation or similar assays to confirm protein interactions (implied).
Main Results:
- CK2α and KIF5C are expressed in late spermatogenesis, while CK2β and TNP1 are found in early spermatogenesis.
- TNP1 is identified as a novel binding partner for the CK2α subunit.
- CK2α, CK2α', TNP1, and KIF5C localize to the sperm acrosome; CK2β localizes to the sperm mid-piece.
Conclusions:
- CK2 subunit combinations and their interactions with TNP1 and KIF5C are crucial for spermatogenesis.
- The distinct localization of CK2 subunits and interacting proteins suggests stage-specific functions.
- KIF5C likely plays a role in protein redistribution during sperm development.
Related Concept Videos
02:15M-Cdk Drives Transition Into Mitosis
Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
02:39Positive Regulator Molecules
Mitotic cell division results in daughter cells that exactly resemble the parent cell. However, errors in the DNA replication or distribution of genetic material may lead to genetic mutations that may be passed down to every new cell formed from the resulting abnormal cell. Propagation of such mutant cells is restricted through checkpoint mechanisms present at different stages of the cell cycle. These checkpoints involve regulator molecules that either promote or demote cell cycle events.
01:22PI3K/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 rapamycin-insensitive companion...
02:34Inhibition of Cdk Activity
The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
01:16Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...