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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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.
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...
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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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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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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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cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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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Updated: Oct 2, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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The STIM1 Phosphorylation Saga.

Fang Yu1, Khaled Machaca1

  • 1Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, USA; Calcium Signaling Group, Research Department, Weill Cornell Medicine Qatar, Doha, Qatar.

Cell Calcium
|February 26, 2022
PubMed
Summary
This summary is machine-generated.

Store-operated Ca2+ entry (SOCE) relies on STIM1 and Orai1. While STIM1 phosphorylation impacts metabolism, its broader physiological roles in cell division and migration remain uncertain.

Keywords:
AMPKCdk1Cell migrationERK/MAPKEndoplasmic ReticulumMeiosisMitosisPhosphorylationSTIM1Serine/threonineStore operated Ca entryTyrosineoocyte

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Time-resolved F&#246;rster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Physiology

Background:

  • Store-operated Ca2+ entry (SOCE) is a crucial calcium influx pathway in metazoans.
  • Defects in SOCE are linked to immunodeficiencies and muscle disorders.
  • The minimal SOCE machinery involves STIM1 (ER sensor) and Orai1 (PM channel).

Purpose of the Study:

  • To review the role and modulation of STIM1 phosphorylation.
  • To critically assess the physiological significance of STIM1 phosphorylation.
  • To clarify the functions of STIM1 phosphorylation in various cellular processes.

Main Methods:

  • Literature review of studies on STIM1 phosphorylation.
  • Analysis of STIM1 phosphorylation under different cellular conditions.
  • Evaluation of evidence linking STIM1 phosphorylation to specific functions.

Main Results:

  • STIM1 is a phosphoprotein, hyper-phosphorylated during cell division.
  • STIM1 phosphorylation is implicated in metabolism, cell division, and migration.
  • Evidence for STIM1 phosphorylation's role in most functions is controversial.

Conclusions:

  • STIM1 phosphorylation clearly modulates cellular energy metabolism.
  • The physiological relevance of STIM1 phosphorylation in other processes like cell division and migration is largely unclear.
  • Further research is needed to elucidate the precise functions of STIM1 phosphorylation.