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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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...
Phosphorylation01:02

Phosphorylation

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...
Phosphate Buffer01:22

Phosphate Buffer

The phosphate buffer system is a critical biological mechanism for maintaining pH stability in the body. This system operates primarily through two components: sodium dihydrogen phosphate (NaH2PO4), which acts as a weak acid, and sodium hydrogen phosphate (Na2HPO4), which serves as a weak base.
Sodium dihydrogen phosphate does not fully dissociate in neutral or acidic solutions. When a strong base, such as sodium hydroxide (NaOH), is introduced into the solution, sodium dihydrogen phosphate...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: Jun 3, 2026

Assaying for Inorganic Polyphosphate in Bacteria
07:20

Assaying for Inorganic Polyphosphate in Bacteria

Published on: January 21, 2019

Phosphate sensing.

Clemens Bergwitz1, Harald Jüppner

  • 1Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA. cbergwitz@partners.org

Advances in Chronic Kidney Disease
|March 17, 2011
PubMed
Summary
This summary is machine-generated.

Human phosphate homeostasis relies on intestinal absorption, bone release, and kidney excretion. Unlike bacteria, how human cells sense phosphate for metabolic and endocrine control remains largely unknown.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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Last Updated: Jun 3, 2026

Assaying for Inorganic Polyphosphate in Bacteria
07:20

Assaying for Inorganic Polyphosphate in Bacteria

Published on: January 21, 2019

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Biochemistry
  • Cell Biology
  • Endocrinology

Background:

  • Human phosphate homeostasis is crucial for cellular functions, tissue growth, and bone mineralization.
  • It involves intestinal absorption, bone resorption, and renal excretion, regulated by parathyroid hormone, vitamin D, and FGF23.
  • Prokaryotes and yeast possess plasma membrane-bound phosphate sensors (pho pathway) absent in metazoans.

Purpose of the Study:

  • To review bacterial and yeast phosphate sensors.
  • To discuss current knowledge on phosphate sensing in multicellular organisms and humans.
  • To explore the mechanisms of metabolic and endocrine phosphate sensing in metazoans.

Main Methods:

  • Literature review of bacterial and yeast phosphate sensing mechanisms.
  • Analysis of database searches for metazoan orthologs of known phosphate sensors.
  • Discussion of existing research on metabolic and endocrine phosphate effects in humans.

Main Results:

  • Bacterial and yeast phosphate sensors are well-characterized but lack identifiable metazoan orthologs.
  • The mechanisms by which human cells sense inorganic phosphate for metabolic and endocrine regulation are largely unknown.
  • It remains unclear if metabolic and endocrine phosphate sensing utilize shared or distinct signaling pathways.

Conclusions:

  • Significant gaps exist in understanding metazoan phosphate sensing compared to simpler organisms.
  • Further research is needed to identify human phosphate sensors and their signaling pathways.
  • Elucidating these mechanisms is vital for understanding phosphate's role in human health and disease.