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Related Concept Videos

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...
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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Updated: Jun 19, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Versatile casein kinase 1: multiple locations and functions.

Jung-Youn Lee1

  • 1Department of Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, USA. lee@dbi.udel.edu

Plant Signaling & Behavior
|October 13, 2009
PubMed
Summary
This summary is machine-generated.

Casein kinase 1 (CK1) proteins regulate essential cellular processes. Arabidopsis CKL6 demonstrates versatile subcellular localization, suggesting diverse roles in plant cell function.

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Last Updated: Jun 19, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
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Area of Science:

  • Plant molecular biology
  • Cellular signaling
  • Protein kinase function

Background:

  • Casein kinase 1 (CK1) proteins are evolutionarily conserved eukaryotic kinases vital for cellular, physiological, and developmental processes.
  • CK1 activity is regulated by spatiotemporal compartmentalization within cells.
  • Plant genomes contain numerous CK1 homologs with largely uncharacterized functions.

Discussion:

  • Arabidopsis CK1-like 6 (CKL6) exhibits unique subcellular targeting mechanisms compared to other CK1s.
  • CKL6's partitioning across different subcellular compartments suggests adaptability.
  • This localization versatility likely underpins CKL6's multiple roles in modulating various cellular targets.

Key Insights:

  • CKL6 displays dynamic subcellular localization within plant cells.
  • The localization patterns of CKL6 are linked to its diverse cellular functions.
  • CKL6 represents a key player in understanding plant-specific CK1 mechanisms.

Outlook:

  • Further research into CKL6's specific cellular targets will elucidate its functions.
  • Investigating CKL6's role in plant development and physiology is warranted.
  • Comparative studies with other plant CK1s can reveal conserved and unique regulatory strategies.