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Related Concept Videos

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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Phosphorylation01:02

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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.
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Phosphoinositides and PIPs01:42

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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.
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Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Transducer Mechanism: Enzyme-Linked Receptors01:27

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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.
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Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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FHA domains: Phosphopeptide binding and beyond.

Ahmad W Almawi1, Lindsay A Matthews1, Alba Guarné1

  • 1Department of Biochemistry and Biomedical Sciences, McMaster University, ON, Canada.

Progress in Biophysics and Molecular Biology
|December 13, 2016
PubMed
Summary

Forkhead-associated (FHA) domains recognize phosphopeptides but also interact through novel interfaces. These interactions, independent of phosphothreonine binding, influence substrate recognition and protein assembly, revealing new FHA domain functions.

Keywords:
Forkhead associated (FHA) domainProtein-protein interactionspThr-binding

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Forkhead-associated (FHA) domains are conserved phosphopeptide recognition modules present in eubacterial and eukaryotic organisms.
  • Initially identified in transcription factors, FHA domains are now known to be part of diverse signaling proteins.
  • Despite low sequence similarity, FHA domains exhibit a conserved structural fold crucial for their function.

Purpose of the Study:

  • To review recent structural and biochemical findings on FHA domains.
  • To highlight novel interaction interfaces discovered on FHA domains.
  • To elucidate the mechanisms by which FHA domains recognize both phosphorylated and non-phosphorylated substrates, and modulate protein oligomerization.

Main Methods:

  • Structural analysis of FHA domains.
  • Biochemical assays to investigate protein-protein interactions.
  • Review of existing literature on FHA domain function and interaction mechanisms.

Main Results:

  • FHA domains possess novel interaction interfaces beyond their canonical phosphopeptide-binding site.
  • These non-canonical interactions are critical for mediating interactions independent of phosphothreonine recognition.
  • FHA domain interactions influence the recognition of diverse substrates and regulate protein oligomerization.

Conclusions:

  • FHA domains exhibit versatile interaction capabilities, extending beyond phosphoprotein recognition.
  • Understanding these novel interfaces is key to comprehending the full spectrum of FHA domain functions in cellular signaling.
  • The interplay of canonical and non-canonical interactions dictates FHA domain activity and downstream cellular events.