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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...
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...
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...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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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Related Experiment Video

Updated: Jun 28, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Phosphorylated HuR shuttles in cycles.

Hyeon Ho Kim1, Myriam Gorospe

  • 1Laboratory of Cellular and Molecular Biology, National Institute on Aging-IRP, National Institutes of Health, Baltimore, Maryland 21224, USA.

Cell Cycle (Georgetown, Tex.)
|October 18, 2008
PubMed
Summary
This summary is machine-generated.

The RNA-binding protein HuR (human antigen R) is regulated by phosphorylation, controlling its movement between the nucleus and cytoplasm. This regulation is crucial for cell proliferation and gene expression during the cell cycle.

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Related Experiment Videos

Last Updated: Jun 28, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The ubiquitous RNA-binding protein HuR (human antigen R) binds mRNAs encoding proliferative proteins.
  • HuR shuttles between the nucleus and cytoplasm, where it stabilizes target mRNAs and modulates translation.
  • Phosphorylation of HuR by Cdk1 at S202 promotes nuclear retention by increasing 14-3-3 binding.

Purpose of the Study:

  • To investigate the role of HuR phosphorylation at residue S242 in regulating HuR's subcellular localization.
  • To determine the impact of S242 phosphorylation on cyclin expression and cell proliferation.

Main Methods:

  • The study focused on post-translational modifications of HuR, specifically phosphorylation at S242.
  • Investigated the effects of these modifications on HuR's nucleocytoplasmic shuttling.
  • Assessed the influence on downstream targets like cyclins and overall cell proliferation.

Main Results:

  • Phosphorylation at residue S242 was identified as a key regulator of HuR's cytoplasmic localization.
  • This modification was shown to influence the expression of cyclins.
  • Modulation of cyclin expression by HuR S242 phosphorylation impacts cell proliferation rates.

Conclusions:

  • HuR phosphorylation at S242 is critical for its cytoplasmic translocation.
  • HuR phosphorylation acts as a mechanism to control gene expression programs in a cell cycle-dependent manner.
  • These findings highlight the importance of post-translational modifications in regulating HuR function and cellular processes.