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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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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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Calmodulin-dependent Signaling01:16

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Published on: October 4, 2024

Modular evolution of phosphorylation-based signalling systems.

Jing Jin1, Tony Pawson

  • 1Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, Canada. jjin@lunenfeld.ca

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|August 15, 2012
PubMed
Summary
This summary is machine-generated.

Protein phosphorylation, regulated by kinases and phosphatases, is crucial for multicellular life. Modular protein evolution, combining domains, drives new functions and can cause diseases like cancer.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Protein phosphorylation is a key regulatory mechanism controlled by protein kinases (writers) and protein phosphatases (erasers).
  • Phospho-binding proteins (readers) recognize phosphorylated sites, mediating downstream signaling events.
  • This writer-reader-eraser system is fundamental to cellular processes and the evolution of multicellularity.

Purpose of the Study:

  • To review the modular organization of signaling proteins involved in phosphorylation.
  • To explore the evolutionary mechanisms driving the development of phosphorylation-based signaling networks.
  • To understand how aberrant domain combinations contribute to diseases like cancer.

Main Methods:

  • Review of existing literature on protein kinases, phosphatases, and phospho-binding proteins.
  • Analysis of modular protein architecture and domain evolution.
  • Examination of evolutionary pathways of signaling networks, including phosphotyrosine signaling.

Main Results:

  • Signaling proteins are modular, composed of binding and catalytic domains that can be recombined through genetic mechanisms.
  • Evolutionary innovations in multicellular animals arose from stepwise changes in domain binding properties and catalytic specificities.
  • Aberrant combinations of these modules can disrupt cell signaling and lead to diseases such as cancer.

Conclusions:

  • The modular nature of signaling proteins has been a major driver of evolutionary innovation, particularly in the development of multicellular organisms.
  • Understanding the evolution of these modular systems provides insights into both normal biological processes and disease pathogenesis.
  • Further research into the interplay of domain shuffling and catalytic activity in signaling networks is warranted.