Source 1primary paper1979The Journal of General Physiology
Toolkit/component II
component II
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Component II is a 12,000-dalton protein identified in frog rod outer segments that undergoes illumination-dependent dephosphorylation. Its phosphorylation state changes as a function of light intensity, with half-maximal and maximal responses reported over defined rhodopsin-bleaching rates.
Usefulness & Problems
Why this is useful
Component II is useful as a native light-responsive biochemical readout in frog rod outer segments because its dephosphorylation tracks illumination intensity. The available evidence supports its use as a marker of photic signaling state rather than as a broadly engineered biological tool.
Problem solved
This protein helps quantify how light exposure is coupled to changes in protein phosphorylation in frog rod outer segments. The evidence does not show that it was developed to solve recombination or synthetic control problems.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
light-induced dephosphorylationTechniques
Computational DesignTarget processes
recombinationInput: Light
Implementation Constraints
The reported context is endogenous frog rod outer segments, where component II was observed as a 12,000-dalton protein. Practical implementation details such as cloning strategy, expression system, cofactors, delivery method, or construct design are not provided in the supplied evidence.
Evidence is limited to a single 1979 study in frog rod outer segments and does not define the molecular identity, sequence, domain architecture, or generalizability of component II. No evidence here supports engineered use, recombination-related function, or computational design.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
molecules per outer segment approximately 10^6
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
bleaching rate for half-maximal dephosphorylation 5000 rhodopsin molecules/outer segment/seconddephosphorylation level approximately half-maximal
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
bleaching rate for maximal dephosphorylation 500000 rhodopsin molecules/outer segment/second
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Approval Evidence
1 source9 linked approval claimsfirst-pass slug component-ii
The proteins, designated component I (13,000 daltons) and component II (12,000 daltons)
Source:
abundancesupports
Each frog rod outer segment contains approximately 10^6 molecules of component I and component II.
Each outer segment contains approximately 10(6( molecules of components I and II.
Source:
dose responsesupports
Illumination bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second causes approximately half-maximal dephosphorylation of components I and II.
Light which bleaches 5.0 x 10(3) rhodopsin molecules/outer segment per second causes approximately half-maximal dephosphorylation.
Source:
dose responsesupports
The extent of light-induced dephosphorylation of components I and II increases with illumination intensity and is maximal at continuous illumination bleaching 5.0 x 10^5 rhodopsin molecules per outer segment per second.
The extent of the light-induced dephosphorylation increases with higher intensities of illumination and is maximal with continuous illumination which bleaches 5.0 x 10(5) rhodopsin molecules/outer segment per second.
Source:
localization behaviorsupports
Components I and II remain associated with fragmented and intact outer segments but dissociate from outer segment membranes under hypoosmotic conditions.
These remain associated with both fragmented and intact outer segments but dissociate from the outer segment membranes under hypoosmotic conditions.
Source:
modulationsupports
Addition of cyclic GMP or cyclic AMP enhances phosphorylation of components I and II in dark-maintained retinas or isolated rod outer segments.
The phosphorylation of components I and II is enhanced by the addition of cyclic GMP or cyclic AMP to either retinas or isolated rod outer segments maintained in the dark.
Source:
modulationsupports
Pharmacological agents that influence cyclic GMP levels in outer segments, including calcium, cause similar effects on phosphorylation of components I and II and on outer segment permeability.
Several pharmacological agents which influence cyclic GMP levels in outer segments, including calcium, cause similar effects on the phosphorylation of components I and II and outer segment permeability.
Source:
reversibilitysupports
Light-induced dephosphorylation of component I and component II is reversible, with rephosphorylation after illumination ceases.
The dephosphorylation is reversible; the two proteins are rephosphorylated when illumination ceases.
Source:
state changesupports
Component I and component II in frog rod outer segments are phosphorylated in the dark and dephosphorylated upon illumination.
Two minor proteins of frog rod outer segments become phosphorylated when retinas are incubated in the dark with 32Pi. The proteins, designated component I (13,000 daltons) and component II (12,000 daltons), are dephosphorylated when retinas are illuminated.
Source:
system dependencesupports
Cyclic nucleotide-stimulated phosphorylation of components I and II is observed in retinas and isolated rod outer segments, whereas light-induced dephosphorylation is observed only in intact retinas.
Although the cyclic nucleotide-stimulated phosphorylation can be observed either in retinas or isolated rod outer segments, the light-induced dephosphorylation is observed only in intact retinas.
Source:
Comparisons
Source-backed strengths
The source reports a measurable dose-response relationship between illumination and dephosphorylation, including an approximately half-maximal response at bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second and a maximal response at 5.0 x 10^5. Component II is also abundant, with approximately 10^6 molecules per frog rod outer segment.
Ranked Citations
- 1.