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Related Concept Videos

Phosphorylation01:02

Phosphorylation

54.5K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Muscles of the Eye01:20

Muscles of the Eye

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The muscles of the eye are sophisticated structures that control eye movement and focus, allowing for the precise and rapid adjustments necessary for vision. The human eye is controlled by ten muscles — six extraocular muscles, three intraocular muscles, and one primary eyelid retractor muscle.
Extraocular Muscles
The six extraocular muscles surround the eyeball and control its movements. They are responsible for a wide range of eye motions, including looking up, down, left, right, and...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Related Experiment Video

Updated: Feb 15, 2026

Optimizing the Setup and Conditions for Ex Vivo Electroretinogram to Study Retina Function in Small and Large Eyes
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Optimizing the Setup and Conditions for Ex Vivo Electroretinogram to Study Retina Function in Small and Large Eyes

Published on: June 27, 2022

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Efferent Innervation to Limulus Eyes In Vivo Phosphorylates a 122 kD Protein.

S C Edwards, A W Andrews, G H Renninger

    The Biological Bulletin
    |January 10, 2018
    PubMed
    Summary

    Horseshoe crab eyes show circadian-controlled changes in light sensitivity. Octopamine triggers a 122 kD protein

    Area of Science:

    • Neuroscience
    • Ophthalmology
    • Circadian Biology

    Background:

    • Efferent fibers innervate horseshoe crab eyes, mediating circadian clock-driven changes.
    • These changes enhance visual sensitivity at night.
    • Octopamine was previously identified as a neurotransmitter stimulating a 122 kD protein phosphorylation via cAMP.

    Purpose of the Study:

    • To investigate the in vivo regulation of 122 kD protein phosphorylation in the lateral eye.
    • To determine the role of this protein in efferent-stimulated visual sensitivity.

    Main Methods:

    • In vivo analysis of 122 kD protein phosphorylation in Limulus lateral eyes.
    • Correlation of phosphorylation with circadian rhythm and efferent nerve stimulation.
    • Immunohistochemical localization of the 122 kD protein.

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    Main Results:

    • 122 kD protein phosphorylation is enhanced in vivo at night, linked to circadian efferent activity.
    • Phosphorylation is also increased during daytime via electrical stimulation of efferent axons.
    • The 122 kD protein is concentrated in photoreceptor-containing tissues.

    Conclusions:

    • Circadian clock and efferent nerve activity regulate 122 kD protein phosphorylation in vivo.
    • This protein is likely involved in the efferent-mediated increase in horseshoe crab retinal sensitivity.