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Phosphorylation

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...

Phosphorylation

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 Phosphatases

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 Phosphatases

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...

Phosphoinositides and PIPs

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Related Experiment Video

Updated: Jun 11, 2026

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

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

Published on: May 3, 2018

Phosphorylation stabilizes Nanog by promoting its interaction with Pin1.

Matteo Moretto-Zita¹, Hua Jin, Zhouxin Shen

¹Section of Molecular Biology and Cell and Developmental Biology, Division of Biological Sciences, University of California, La Jolla, CA 92093-0322, USA.

Proceedings of the National Academy of Sciences of the United States of America

|July 13, 2010

Summary

Embryonic stem cells (ESCs) self-renewal is maintained by Nanog protein stabilization. Phosphorylation of Nanog by Pin1 prevents its degradation, crucial for stem cell pluripotency and therapy potential.

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Related Experiment Videos

Last Updated: Jun 11, 2026

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

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

Published on: May 3, 2018

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Area of Science:

Stem cell biology
Molecular and cell biology

Background:

Embryonic stem cells (ESCs) possess self-renewal and pluripotency, making them vital for regenerative medicine.
Understanding the molecular mechanisms governing ESC self-renewal is critical for therapeutic applications.

Purpose of the Study:

To elucidate the post-translational modifications regulating Nanog, a key transcription factor for ESC self-renewal.
To investigate the role of prolyl isomerase Pin1 in Nanog stabilization and its impact on ESC function.

Main Methods:

Analysis of Nanog phosphorylation at Ser/Thr-Pro motifs.
Investigation of the interaction between Nanog and Pin1 using biochemical assays.
Assessment of ESC self-renewal and teratoma formation upon inhibition of Pin1 activity or Nanog-Pin1 interaction.

Main Results:

Nanog is phosphorylated at multiple Ser/Thr-Pro sites, facilitating its interaction with Pin1.
Pin1-mediated stabilization of Nanog suppresses its ubiquitination and degradation.
Inhibition of Pin1 or disruption of the Nanog-Pin1 interaction impairs ESC self-renewal and teratoma formation.

Conclusions:

Post-translational modification, specifically phosphorylation by Pin1, is a critical mechanism for maintaining Nanog stability in ESCs.
This regulatory pathway is essential for preserving the self-renewal capacity and pluripotency of embryonic stem cells.
Targeting the Nanog-Pin1 interaction could offer new strategies for controlling stem cell behavior in therapeutic contexts.