Related Experiment Video

Updated: Aug 9, 2026

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death
09:18

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Published on: December 27, 2016

Acrylamide treatment of PtK1 cells causes dephosphorylation of keratin polypeptides

B S Eckert1, P L Yeagle

  • 1Department of Anatomical Sciences, School of Medicine, State University of New York, Buffalo 14214.

Cell Motility and the Cytoskeleton
|January 1, 1988
PubMed

Insights

Acrylamide treatment disrupts keratin filament distribution in PtKl cells, linked to rapid dephosphorylation. Reversible effects suggest protein phosphorylation regulates keratin organization.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Cytoskeleton Dynamics

Background:

  • Keratin filaments form crucial intermediate filament networks in epithelial cells.
  • The dynamic regulation of keratin organization is essential for cellular structure and function.
  • Protein phosphorylation is a key post-translational modification involved in cellular signaling and structural protein regulation.

Purpose of the Study:

  • To investigate the impact of acrylamide on keratin filament distribution in PtKl cells.
  • To examine the role of keratin phosphorylation in response to acrylamide treatment.
  • To elucidate the relationship between keratin phosphorylation dynamics and filament organization.

Main Methods:

  • PtKl cells were treated with acrylamide to observe morphological changes.
  • Cellular keratins were labeled with 32P to assess phosphorylation levels.
  • 31P Nuclear Magnetic Resonance (NMR) spectroscopy was used to analyze inorganic phosphate levels.
  • Keratin phosphorylation turnover rates were determined.

Main Results:

  • Acrylamide treatment caused reversible alterations in keratin filament distribution.
  • Four keratins (56, 53, 45, and 40 kDa) were identified as phosphorylated.
  • Acrylamide induced rapid dephosphorylation of keratins (50% decrease in 2 hr).
  • A transient decrease and subsequent increase in inorganic phosphate were observed during acrylamide treatment.

Conclusions:

  • Keratin phosphorylation is strongly correlated with the morphological response of keratin filaments to acrylamide.
  • Protein phosphorylation plays a significant role in mediating the normal distribution of keratin filaments.
  • The dynamic phosphorylation state of keratins is critical for maintaining cytoskeletal integrity.

More Related Videos

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

Related Concept Videos

Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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...
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...