Tag: Phosphorylation
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Marx SO, Reiken S, Hisamatsu Y, Gaburjakova M, Gaburjakova J, Yang YM, Rosemblit N, Marks AR. Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers. J Cell Biol. 2001 May 14;153(4):699-708. doi: 10.1083/jcb.153.4.699. PMID: 11352932; PMCID: PMC2192391.
Abstract Ryanodine receptors (RyRs), intracellular calcium release channels required for cardiac and skeletal muscle contraction, are macromolecular complexes that include kinases and phosphatases. Phosphorylation/dephosphorylation plays a key role in regulating the function of many ion channels, including RyRs. However, the mechanism by which kinases and phosphatases are targeted to ion channels is not well understood.…
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Steroidogenic factor 1 (SF-1) protein and a few related things
The steroidogenic factor 1 (SF-1) protein is a transcription factor involved in sex determination by controlling the activity of genes related to the reproductive glands or gonads and adrenal glands. This protein is encoded by the NR5A1 gene, a member of the nuclear receptor subfamily, located on the long arm of chromosome 9 at position 33.3. It was originally identified as a regulator of genes encoding cytochrome P450 steroid hydroxylases, however, further roles…
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Structure of DNA repair protein XRCC4 aka X-ray repair cross-complementing protein 4
XRCC4 protein is a TETRAMER that resembles the shape of a DUMBBELL containing two globular ends separated by a long, thin stalk. The tetramer is composed of two dimers, and each dimer is made up of two similar subunits. The first subunit (L) contains amino acid residues 1 – 203 and has a longer stalk than the second…
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Vitellin is essential in the fertilization process, and embryonic development in egg-laying organisms
Vitellin is a protein found in the egg yolk. It is a phosphoprotein. Vitellin is a generic name for major of many yolk proteins. Vitellin has been known since the 1900s. The periodic acid-Schiff method and Sudan black B dye was used to help determine that Vitellin is a glycolipoprotein because it stained positive when tested. This protein was…
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Protein phosphorylation was first reported in 1906
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by…
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Phosphorylation
In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion.[1] This process and its inverse, dephosphorylation, are common in biology.[2] Protein phosphorylation often activates (or deactivates) many enzymes.[3][4] During respiration and photosynthesis Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the “high-energy” exchange medium in the cell. During aerobic respiration, ATP is synthesized…
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