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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...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
Negative Regulator Molecules01:23

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
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...

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Related Experiment Video

Updated: May 21, 2026

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

Phosphorylation puts the pRb tumor suppressor into shape.

Andreas M F Heilmann1, Nicholas J Dyson

  • 1Massachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA.

Genes & Development
|June 5, 2012
PubMed
Summary
This summary is machine-generated.

Phosphorylation alters the structure of retinoblastoma protein (pRb) at specific sites. These changes modify how pRb interacts with E2F, offering precise control over cellular processes.

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Last Updated: May 21, 2026

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Analysis of Cell Cycle Position in Mammalian Cells
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Analysis of Cell Cycle Position in Mammalian Cells

Published on: January 21, 2012

Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • Protein Structure and Function

Background:

  • The retinoblastoma protein (pRb) is a critical tumor suppressor that regulates the cell cycle.
  • pRb controls cell cycle progression by binding to and inhibiting transcription factors like E2F.
  • Post-translational modifications, such as phosphorylation, are known to regulate pRb activity.

Purpose of the Study:

  • To elucidate the structural mechanisms by which phosphorylation at specific sites (T373 and S608) alters retinoblastoma protein (pRb) structure.
  • To understand how these structural changes impact the interaction between pRb and its target E2F.
  • To explore the functional implications of distinct phosphorylation events on pRb conformation and activity.

Main Methods:

  • X-ray crystallography to determine the structures of pRb with specific phosphorylation events.
  • Biochemical assays to assess the binding affinity and interaction dynamics between pRb and E2F.
  • Conformational analysis to identify structural changes induced by phosphorylation.

Main Results:

  • Phosphorylation at T373 and S608 induces distinct conformational changes in pRb structure.
  • These modifications lead to altered pRb-E2F interactions through two separate mechanisms.
  • The study reveals how specific phosphorylation sites act as regulatory tools to precisely sculpt pRb function.

Conclusions:

  • Specific phosphorylation sites on pRb provide a versatile mechanism for fine-tuning its structure and function.
  • Understanding these phosphorylation-dependent structural changes is crucial for comprehending cell cycle control and tumor suppression.
  • The findings offer insights into potential therapeutic strategies targeting pRb in cancer treatment.