Related Experiment Video
Updated: Jun 22, 2025

08:05
Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
18.4K
NUAK: never underestimate a kinase
George L Skalka1,2, Declan Whyte2, Dominika Lubawska1
1School of Cancer Sciences, University of Glasgow, Glasgow, U.K.
Essays in Biochemistry
|June 28, 2024
Summary
NUAK1 and NUAK2 kinases, though activated by LKB1, promote tumor growth. This review details their functions, regulation, and downstream targets in cancer progression.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- NUAK1 and NUAK2 are kinases structurally related to AMP-activated protein kinase (AMPK) complexes.
- These kinases are typically activated by the tumor suppressor kinase LKB1.
- Both NUAK1 and NUAK2 have been implicated in promoting tumor development and progression.
Purpose of the Study:
- To review the structural and functional similarities between NUAK1 and NUAK2.
- To discuss the regulation of NUAK1 and NUAK2 at the gene, transcript, and protein levels.
- To examine the downstream targets phosphorylated by NUAKs and their role in cancer-related signaling pathways.
Main Methods:
- Literature review of existing studies on NUAK1 and NUAK2.
- Analysis of gene, transcript, and protein regulation mechanisms.
- Discussion of kinase activity and downstream signaling pathways.
Main Results:
- NUAK1 and NUAK2 share structural and functional similarities.
- Their regulation is complex, occurring at multiple levels.
- They phosphorylate specific targets involved in pathways that promote tumor progression.
Conclusions:
- NUAK1 and NUAK2 play significant roles in cancer development and progression.
- Understanding their regulation and downstream effects is crucial for targeted cancer therapies.
- Further research into NUAK1 and NUAK2 signaling pathways may reveal new therapeutic strategies.
Related Concept Videos
Protein Kinases and Phosphatases
13.1K
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
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
MAPK Signaling Cascades
5.4K
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...
5.4K
PI3K/mTOR/AKT Signaling Pathway
3.5K
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...
3.5K
Calmodulin-dependent Signaling
5.1K
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,...
5.1K
The JAK-STAT Signaling Pathway
8.8K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
8.8K
Amplifying Signals via Enzymatic Cascade
8.5K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.5K

