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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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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.
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Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
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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 the...
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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.
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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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Published on: August 13, 2012

BRCT domains: phosphopeptide binding and signaling modules.

Maria C Rodriguez1, Zhou Songyang

  • 11Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.

Frontiers in Bioscience : a Journal and Virtual Library
|May 30, 2008
PubMed
Summary

The BRCA1 C-terminus (BRCT) domains are crucial for tumor suppression and act as phosphopeptide binding sites. This review details their structure, function, and role in DNA repair networks.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The BRCA1 C-terminus (BRCT) domains are vital for BRCA1's tumor suppressor activity.
  • BRCT domains are conserved across species and are present in various proteins.
  • Recent research identifies BRCT domains as novel phosphopeptide binding regions.

Purpose of the Study:

  • To review recent biochemical and structural data on BRCT domain function.
  • To elucidate the molecular basis of BRCT-mediated interactions.
  • To emphasize the role of phospho-specific interactions in DNA repair.

Main Methods:

  • Literature review of biochemical and structural studies.
  • Analysis of protein domain interactions.
  • Bioinformatic predictions of novel binding sites.

Main Results:

  • BRCT domains function as phosphopeptide binding modules.
  • Phospho-specific interactions mediated by BRCT domains are critical in DNA repair pathways.
  • Structural data reveals the molecular mechanisms of BRCT domain binding.

Conclusions:

  • BRCT domains are key regulators of DNA repair through phospho-specific interactions.
  • Further research may identify additional BRCT domains and their binding partners.
  • Understanding BRCT domain function has implications for cancer research.