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

Phosphorylation01:02

Phosphorylation

51.3K
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...
51.3K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.5K
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...
13.5K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

4.0K
The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
4.0K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

9.9K
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...
9.9K
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

7.3K
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
7.3K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.3K
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,...
5.3K

You might also read

Related Articles

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

Sort by
Same author

Anti-CRISPR-mediated continuous directed evolution of CRISPR-Cas9 in human cells.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Targeting the H/KRAS α4-β6-α5 Allosteric Lobe with Macrocyclic Peptides.

ACS medicinal chemistry letters·2026
Same author

Proximity-Induced Rewiring of Oncogenic Kinase Triggers Apoptosis.

ACS central science·2026
Same author

Lysine Targeting Group-Transfer Chimeras for Proximity Induction.

Angewandte Chemie (International ed. in English)·2026
Same author

Nuclear Localization Signals Enable the Cellular Delivery of an Anti-CRISPR Protein to Control Genome Editing.

bioRxiv : the preprint server for biology·2025
Same author

Ultrasmall Chemogenetic Tags with Group-Transfer Ligands.

Angewandte Chemie (International ed. in English)·2025
Same journal

A human-specific genetic modifier reconfigures large-scale cortical network dynamics underlying behavioral performance.

bioRxiv : the preprint server for biology·2026
Same journal

<i>Staphylococcus aureus</i> uses a eukaryotic-like uridyltransferase to make UDP-GlcNAc for cell wall synthesis.

bioRxiv : the preprint server for biology·2026
Same journal

Dynamic redistribution of eIF4F controls cap-dependent translation initiation.

bioRxiv : the preprint server for biology·2026
Same journal

When does additional information improve accuracy of RNA secondary structure prediction?

bioRxiv : the preprint server for biology·2026
Same journal

Normative brain-state trajectories reveal deviation from healthy aging in Alzheimer's disease.

bioRxiv : the preprint server for biology·2026
Same journal

Noradrenergic infraslow rhythm during sleep is the critical link between heart-rate dynamics and memory consolidation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Sep 19, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.5K

Phosphorylation-inducing molecules for regulating dynamic cellular processes.

Rajaiah Pergu, Sreekanth Vedagopuram, Praveen Kokkonda

    Biorxiv : the Preprint Server for Biology
    |June 4, 2025
    PubMed
    Summary
    This summary is machine-generated.

    A new platform using phosphorylation-inducing chimeric small molecules (PHICS) enables targeted protein phosphorylation under physiological conditions. This advance controls cellular processes like oncogenic signaling and neuronal phase separation with precision.

    More Related Videos

    Identification of Kinase-substrate Pairs Using High Throughput Screening
    11:13

    Identification of Kinase-substrate Pairs Using High Throughput Screening

    Published on: August 29, 2015

    8.3K
    A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
    10:17

    A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

    Published on: April 29, 2022

    2.5K

    Related Experiment Videos

    Last Updated: Sep 19, 2025

    Oligopeptide Competition Assay for Phosphorylation Site Determination
    09:16

    Oligopeptide Competition Assay for Phosphorylation Site Determination

    Published on: May 18, 2017

    8.5K
    Identification of Kinase-substrate Pairs Using High Throughput Screening
    11:13

    Identification of Kinase-substrate Pairs Using High Throughput Screening

    Published on: August 29, 2015

    8.3K
    A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
    10:17

    A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

    Published on: April 29, 2022

    2.5K

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Medicine

    Background:

    • Protein phosphorylation is crucial for cellular signaling and information transfer.
    • Existing Phosphorylation-Inducing Chimeric Small Molecules (PHICS) have limitations including serum starvation, target overexpression, limited complex recruitment, and poor control.

    Purpose of the Study:

    • To develop an improved AMPK PHICS platform for targeted protein phosphorylation.
    • To enable PHICS application under physiological conditions with enhanced control and broader complex recruitment.

    Main Methods:

    • Development of a novel AMPK PHICS platform.
    • Demonstration of platform utility in controlling oncogenic signaling and neuronal phase separation.
    • Application of PHICS to target Bruton's Tyrosine Kinase (BTK) and Liprin-α3.

    Main Results:

    • The new PHICS platform operates without serum starvation or target overexpression.
    • It recruits multiple AMP-activated protein kinase (AMPK) complexes and offers dose and temporal control.
    • PHICS targeting BTK induced death in drug-resistant cancer cells by attenuating oncogenic signaling.
    • PHICS targeting Liprin-α3 controlled neuronal phase separation.

    Conclusions:

    • The developed AMPK PHICS platform overcomes limitations of previous systems.
    • It provides precise control over protein phosphorylation for dynamic cellular processes.
    • This platform holds significant potential for basic research and biomedical applications.