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Related Concept Videos

Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
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,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.

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Related Experiment Video

Updated: May 22, 2026

An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
11:20

An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation

Published on: August 30, 2017

Uncaging akt.

Sean J Humphrey1, David E James

  • 1Diabetes and Obesity Program, Garvan Institute of Medical Research, Darlinghurst, New South Wales 2010, Australia.

Science Signaling
|May 10, 2012
PubMed
Summary
This summary is machine-generated.

Adenosine triphosphate (ATP) binding to Akt protein kinase creates a protective cage around its phosphorylation sites, regulating its activity. ATP hydrolysis and substrate phosphorylation release the kinase, allowing dephosphorylation and inactivation.

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Last Updated: May 22, 2026

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Signaling

Background:

  • Protein kinase cascades are central to signal transduction pathways.
  • Kinase activity is typically regulated by phosphorylation and dephosphorylation.
  • Akt protein kinase activation involves phosphorylation at two key regulatory sites.

Purpose of the Study:

  • To elucidate the role of nucleotide binding in protein kinase regulation.
  • To investigate the mechanism by which adenosine triphosphate (ATP) binding affects Akt kinase activity.
  • To understand the interplay between phosphorylation, dephosphorylation, and nucleotide binding in kinase control.

Main Methods:

  • The study focuses on the Akt protein kinase.
  • Investigated the structural and functional consequences of adenosine triphosphate (ATP) binding.
  • Examined the impact of ATP hydrolysis and substrate phosphorylation on kinase activity and regulation.

Main Results:

  • Adenosine triphosphate (ATP) binding to Akt induces an intramolecular interaction, forming a 'cage' around its phosphorylation sites.
  • This cage restricts phosphatase access, maintaining kinase activation.
  • ATP hydrolysis and subsequent substrate phosphorylation trigger the opening of this cage, permitting dephosphorylation and kinase inactivation.

Conclusions:

  • A novel layer of kinase regulation involving nucleotide binding has been identified.
  • The findings reveal a switch-like mechanism controlling Akt kinase activity through a phosphorylation-site cage.
  • This mechanism provides critical new insights into the dynamic regulation of protein kinases in cellular signaling.