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

Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

19.6K
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...
19.6K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

8.0K
Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
8.0K
Diversity in Cell Signaling Responses01:22

Diversity in Cell Signaling Responses

8.8K
The physiological function of a cell and cellular communication are outcomes of a range of extrinsic signals, intracellular signaling pathways, and cellular responses. No two cell types express the same repertoire of signaling components. Receptors are highly selective for their cognate ligands, but once activated, they can alter multiple cellular processes such as DNA transcription, protein synthesis, and metabolic activity. 
Graded and Abrupt Responses
Some signaling systems generate...
8.8K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.2K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.2K
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

55.6K
Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
55.6K
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

37.3K
37.3K

You might also read

Related Articles

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

Sort by
Same author

Wave-optics simulation model for full-field modulation-based tensor tomography using a random wavefront modulator.

Optics express·2026
Same author

STING dampens the unfolded protein response to enable the presentation of self-antigens on MHC-I during inflammation.

Cell reports·2026
Same author

LRRK2 mutations block NCOA4 trafficking upon iron overload leading to ferroptotic death.

Journal of cell science·2026
Same author

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

ACS medicinal chemistry letters·2026
Same author

Relation of blood-based inflammation conditional networks to key immune health status and Alzheimer's biomarkers in aging adults.

Neurobiology of aging·2026
Same author

Noncanonical Transcription and Splicing Shape the Colorectal Cancer Immunopeptidome in MSI and MSS Tumors.

Molecular & cellular proteomics : MCP·2026

Related Experiment Video

Updated: Apr 17, 2026

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

8.7K

A cell-signaling network temporally resolves specific versus promiscuous phosphorylation.

Evgeny Kanshin1, Louis-Philippe Bergeron-Sandoval2, S Sinan Isik2

  • 1Département de Biochimie, Université de Montréal, C.P. 6128, Succursale centre-ville, Montréal, QC H3C 3J7, Canada; Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128, Succursale centre-ville, Montréal, QC H3C 3J7, Canada.

Cell Reports
|February 24, 2015
PubMed
Summary

Functional phosphorylation changes occur rapidly, within 60 seconds, on specific substrates compared to promiscuous ones. This study reveals new insights into yeast cell cycle and morphogenesis regulation.

More Related Videos

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

3.0K
Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K

Related Experiment Videos

Last Updated: Apr 17, 2026

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

8.7K
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

3.0K
Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K

Area of Science:

  • Molecular Biology
  • Cellular Dynamics
  • Proteomics

Background:

  • Kinase and phosphatase interactions govern cellular signaling through phosphorylation.
  • Understanding the kinetics of specific versus promiscuous substrate interactions is crucial for deciphering signaling pathways.
  • The high-osmolarity glycerol (HOG) response in Saccharomyces cerevisiae serves as a model for studying rapid cellular adaptation.

Purpose of the Study:

  • To test the hypothesis that optimized kinase- or phosphatase-substrate interactions lead to faster phosphorylation changes.
  • To develop and apply a high temporal resolution phosphoproteomics protocol to analyze dynamic phosphosites.
  • To investigate the kinetics of phosphorylation events during the HOG response in yeast.

Main Methods:

  • Development of a high temporal resolution global phosphoproteomics protocol.
  • Application of the protocol to study the HOG response in Saccharomyces cerevisiae.
  • Quantitative analysis of phosphoproteome changes and phosphodynamics at sub-minute resolution.

Main Results:

  • The developed method enables accurate, stimulus-specific measurement of phosphoproteome changes with high temporal resolution.
  • Rates of evolution for dynamic phosphosites were comparable to known functional phosphosites and lower than static ones.
  • Kinetic profile analyses demonstrated that functional kinase- or phosphatase-substrate interactions occur rapidly (within 60 s) compared to promiscuous interactions.

Conclusions:

  • Specific and functional kinase- or phosphatase-substrate interactions are kinetically distinct from promiscuous interactions.
  • Rapid phosphorylation events (<60 s) are indicative of functional signaling pathways.
  • Identified phosphorylation changes in cytoskeletal and mitotic spindle proteins suggest roles in cell cycle and morphogenesis regulation.