Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

9.8K
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...
9.8K
Activation of Integrins01:15

Activation of Integrins

4.6K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
4.6K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.3K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
3.3K
Integrins01:10

Integrins

4.9K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.9K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

13.7K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
13.7K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

15.7K
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...
15.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The phosphatase PPM1F, a negative regulator of integrin activity, is essential for embryonic development and controls tumor cell invasion.

BMC biology·2025
Same author

A quinolone N-oxide antibiotic selectively targets Neisseria gonorrhoeae via its toxin-antitoxin system.

Nature microbiology·2025
Same author

Current investigation of carcinoembryonic antigen cell adhesion molecule (CEACAM) biology summary of the 32nd CEA symposium: 20-23 September 2024. Würzburg, Germany.

European journal of clinical investigation·2024
Same author

Structural insights into a DNA polymerase reading the xeno nucleic acid HNA.

Nucleic acids research·2024
Same author

Structures of a DNA Polymerase Caught while Incorporating Responsive Dual-Functional Nucleotide Probes.

Angewandte Chemie (International ed. in English)·2024
Same author

A flexible loop in the paxillin LIM3 domain mediates its direct binding to integrin β subunits.

PLoS biology·2024
Same journal

A pan-vertebrate signaling motif controls the molecular function of intracellular AQP12.

The Journal of cell biology·2026
Same journal

Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.

The Journal of cell biology·2026
Same journal

Recruitment and release of XPG during NER is controlled by pre- and post-incision factors and EXO1.

The Journal of cell biology·2026
Same journal

Meiotic CENP-C supports centromere assembly and kinetochore recruitment in spermatogenesis.

The Journal of cell biology·2026
Same journal

Phosphatidylserine and RhoB connect PI4P and PA metabolism to maintain plasma membrane identity.

The Journal of cell biology·2026
Same journal

PIKfyve influences inter-organelle contacts with lysosomes to modulate the endoplasmic reticulum.

The Journal of cell biology·2026
See all related articles

Related Experiment Video

Updated: Dec 3, 2025

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation
04:15

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation

Published on: February 2, 2024

2.2K

PPM1F controls integrin activity via a conserved phospho-switch.

Tanja M Grimm1,2, Nina I Dierdorf1,2, Karin Betz2,3

  • 1Lehrstuhl Zellbiologie, Fachbereich Biologie, Universität Konstanz, Konstanz, Germany.

The Journal of Cell Biology
|October 29, 2020
PubMed
Summary
This summary is machine-generated.

The phosphatase PPM1F controls integrin activity by dephosphorylating a key motif. PPM1F deficiency leads to increased integrin activation, impacting cell adhesion and embryonic development.

More Related Videos

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

15.6K
Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

Published on: March 8, 2017

8.8K

Related Experiment Videos

Last Updated: Dec 3, 2025

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation
04:15

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation

Published on: February 2, 2024

2.2K
Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

15.6K
Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

Published on: March 8, 2017

8.8K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrin activity is crucial for development and tissue health.
  • Dysregulated integrin function is implicated in various diseases.
  • Phosphorylation of the integrin β cytoplasmic domain at T788/T789 enhances integrin activity.

Purpose of the Study:

  • To identify the enzyme responsible for dephosphorylating the integrin β T788/T789 motif.
  • To elucidate the role of this enzyme in regulating integrin activity and cellular processes.
  • To investigate the in vivo consequences of disrupting this regulatory pathway.

Main Methods:

  • Genetic screening to identify phosphatases.
  • In vitro biochemical assays to confirm enzyme activity.
  • Analysis of cell lines with disrupted PPM1F gene.
  • Phenotypic analysis of knockout mice.

Main Results:

  • The phosphatase PPM1F was identified as the enzyme that selectively dephosphorylates the integrin β T788/T789 motif.
  • PPM1F acts as a phospho-switch, determining interactions with integrin activators (talin, kindlin-2) or suppressors (filaminA).
  • PPM1F-deficient cells exhibit constitutive integrin phosphorylation, increased activity, and enhanced adhesion; these phenotypes are reversible.
  • ppm1f gene disruption in mice causes embryonic lethality at E10.5.

Conclusions:

  • PPM1F is the critical enzyme controlling the T788/T789 phospho-switch in the integrin β1 cytoplasmic tail.
  • PPM1F acts as a novel regulator of integrin activity.
  • PPM1F represents a potential therapeutic target for modulating integrin function in disease.