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Related Concept Videos

Calmodulin-dependent Signaling01:16

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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.
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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,...
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Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
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Related Experiment Video

Updated: Aug 13, 2025

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
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SGC-CAMKK2-1: A Chemical Probe for CAMKK2.

Carrow Wells1, Yi Liang1, Thomas L Pulliam2

  • 1Structural Genomics Consortium, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Cells
|January 21, 2023
PubMed
Summary

Researchers developed SGC-CAMKK2-1, a selective chemical probe for calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2). This new tool aids in studying CAMKK2

Keywords:
CAMKK2NanoBRETchemical probekinasekinase selectivity

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Area of Science:

  • Biochemistry and Molecular Biology
  • Pharmacology and Drug Discovery

Background:

  • Calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2) is a serine/threonine kinase involved in crucial biological functions.
  • Limited availability of selective inhibitors hinders the therapeutic investigation of CAMKK2.
  • Developing specific chemical tools is essential to explore CAMKK2's role in disease and potential treatments.

Purpose of the Study:

  • To disclose a novel, selective small molecule inhibitor for CAMKK2.
  • To provide a chemical probe for interrogating the biological functions of CAMKK2.
  • To facilitate research demonstrating the therapeutic potential of CAMKK2 inhibition.

Main Methods:

  • Chemical synthesis and characterization of small molecules.
  • Biochemical assays to determine kinase inhibition potency and selectivity.
  • Validation of the chemical probe's efficacy in relevant biological systems.

Main Results:

  • Successful identification and disclosure of SGC-CAMKK2-1, a selective chemical probe targeting CAMKK2.
  • Demonstration of SGC-CAMKK2-1's high selectivity for CAMKK2 over other kinases.
  • Establishment of SGC-CAMKK2-1 as a valuable tool for CAMKK2 research.

Conclusions:

  • SGC-CAMKK2-1 represents a significant advancement in the field of CAMKK2 research.
  • This selective probe will enable deeper understanding of CAMKK2's biological roles.
  • The availability of SGC-CAMKK2-1 supports the exploration of CAMKK2 as a therapeutic target.