Source 1primary paper1979The Journal of General Physiology
Toolkit/component I
component I
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Component I is a 13,000-dalton phosphoprotein identified in frog rod outer segments that undergoes light-induced dephosphorylation. In the cited 1979 study, it was characterized as an abundant outer-segment-associated protein whose phosphorylation state changes as a function of illumination intensity.
Usefulness & Problems
Why this is useful
Component I is useful as a native biochemical readout of light-responsive signaling in frog rod outer segments because its dephosphorylation scales with illumination. The available evidence supports its use as a marker of photic response magnitude rather than as an engineered optogenetic actuator or modular protein domain.
Problem solved
This protein helps address the problem of measuring endogenous light-dependent biochemical state changes in vertebrate photoreceptor outer segments. Specifically, the cited work links component I dephosphorylation to defined rhodopsin bleaching rates, providing a quantitative correlate of illumination intensity.
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 supplied evidence places component I in frog rod outer segments and identifies it as a 13,000-dalton protein responsive to illumination. No practical implementation details are provided for heterologous expression, delivery, cofactor requirements, or construct engineering.
The evidence is limited to a single cited study in frog rod outer segments and does not establish component I as an engineered tool, transferable module, or recombination regulator. No sequence, structure, domain boundaries, construct design, or independent validation data are provided in the supplied evidence.
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-i
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
Component I was reported to be abundant, with approximately 10^6 molecules per frog rod outer segment together with component II, which supports biochemical detectability. Its dephosphorylation showed a dose response to light, with approximately half-maximal response at bleaching 5.0 x 10^3 rhodopsin molecules per outer segment per second and maximal response at 5.0 x 10^5 rhodopsin molecules per outer segment per second.
Ranked Citations
- 1.