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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...
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...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Phosphoinositides and PIPs01:42

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...
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...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...

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Related Experiment Video

Updated: May 7, 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

PTPL1: a large phosphatase with a split personality.

Ogan D Abaan1, Jeffrey A Toretsky

  • 1Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC 20057, USA.

Cancer Metastasis Reviews
|February 13, 2008
PubMed
Summary
This summary is machine-generated.

Protein tyrosine phosphatase PTPL1 is the largest non-receptor PTP. Its complex structure suggests diverse roles in cancer, acting as both a tumor promoter and suppressor depending on context.

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Last Updated: May 7, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
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Published on: July 17, 2020

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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Protein tyrosine phosphatase PTPL1 (also known as PTPN13, FAP-1, PTP-BAS, PTP1E) is the largest non-receptor type PTP.
  • PTPL1 possesses a complex structure with a PTP domain and at least 7 other interaction domains, suggesting multifaceted cellular roles.

Purpose of the Study:

  • To elucidate the complex and context-dependent roles of PTPL1 in cancer.
  • To understand how PTPL1's structure influences its function in cellular processes like growth, stress response, and cytoskeletal remodeling.

Main Methods:

  • Analysis of PTPL1's structural domains and their implications for molecular interactions.
  • Review of existing experimental studies investigating PTPL1's function in cancer cell biology.

Main Results:

  • PTPL1's structural complexity suggests modulation of diverse cellular functions.
  • Conflicting evidence exists regarding PTPL1's role in cancer, with studies indicating both tumor-promoting and tumor-suppressing activities.

Conclusions:

  • The function of PTPL1 in cancer is complex and context-dependent.
  • Further research into PTPL1's molecular complexes, interaction partners, substrates, regulation, and localization is crucial for understanding its multifaceted roles.