Source 1primary paper2017Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics
Toolkit/photo-activatable Akt probe
photo-activatable Akt probe
Also known as: PA-Akt, PA-Akt probe
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The photo-activatable Akt probe (PA-Akt) is a light-controlled multi-component Akt activation system built from the plant CRY2-CIB1 light-inducible interaction module. Upon illumination, it activates Akt signaling with sequential phosphorylation of Akt at S473 and T308 and engages downstream GSK-3β signaling in a light-intensity-dependent manner.
Usefulness & Problems
Why this is useful
PA-Akt provides optical control over Akt pathway activation, enabling easy, transient, and repeatable induction of endogenous Akt signaling. The reported system is useful for studying Akt-dependent cell physiology and cancer-related signaling under temporally controlled stimulation.
Source:
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Problem solved
This tool addresses the need for noninvasive temporal control of Akt activation without constitutive pathway perturbation. It specifically enables experimental induction of Akt signaling to examine consequences such as stress protection under nutritional deprivation and H2O2 exposure.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
PA-Akt is based on the plant cryptochrome2 (CRY2) and cryptochrome-interacting basic helix-loop-helix protein CIB1, indicating a multi-component construct design using a light-inducible interaction pair. The provided evidence does not specify illumination wavelength, construct architecture beyond the CRY2-CIB1 basis, expression system, or delivery method.
The supplied evidence comes from a single 2017 source and provides limited implementation and benchmarking detail. Independent replication, quantitative performance metrics, wavelength specifications, and validation across diverse models are not established in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug photo-activatable-akt-probe
a newly developed photo-activatable Akt (PA-Akt) probe, based on a light-inducible protein interaction module of plant cryptochrome2 (CRY2) and cryptochrome-interacting basic helix-loop-helix (CIB1)
Source:
activation effectsupports
Light illumination sequentially phosphorylates S473 and T308 of probe-Akt.
Western blot analysis revealed that S473 and T308 of the Akt of probe-Akt were sequentially phosphorylated by intermittent and continuous light illumination.
Source:
cell protection effectsupports
Photo-activated Akt significantly protects cells against nutritional deprivation and H2O2 stress.
The photo-activated Akt conferred protection against nutritional deprivation and H₂O₂ stresses to the cells significantly.
Source:
operational propertysupports
The PA-Akt probe enables endogenous Akt activation that is easy, transient, and repeatable.
Using the newly developed PA-Akt probe, endogenous Akt was activated easily, transiently, and repeatedly.
Source:
pathway activationsupports
Photo-activation of the PA-Akt probe activates endogenous Akt and its downstream signal GSK-3β in a light-intensity-dependent manner.
Endogenous Akt and GSK-3β, one of the main downstream signals of Akt, were also phosphorylated, depending on light intensity. These facts indicate that photo-activation of probe-Akt can activate endogenous Akt and its downstream signals.
Source:
tool mechanismsupports
Blue light causes the PA-Akt probe component CRY2-Akt to interact with Myr-CIBN and anchor at the cell membrane.
By illuminating blue light to the cells stably transfected with PA-Akt probe, CRY2-Akt (a fusion protein of CRY2 and Akt) underwent a structural change and interacted with Myr-CIBN (myristoylated N-terminal portion of CIB1), anchoring it at the cell membrane.
Source:
Comparisons
Source-backed strengths
The reported probe supports light-triggered sequential phosphorylation of Akt at S473 and T308, indicating ordered activation of the pathway. It was also reported to protect cells against nutritional deprivation and H2O2 stress, and its activation was described as easy, transient, and repeatable.
Ranked Citations
- 1.