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

cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

7.3K
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
7.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

4.7K
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,...
4.7K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

3.3K
3.3K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

12.2K
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...
12.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.6K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.6K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

7.7K
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...
7.7K

You might also read

Related Articles

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

Sort by
Same author

The RNA-binding protein PRRC2B preserves 5' TOP mRNA during starvation to maintain ribosome biogenesis during nutrient recovery.

Nucleic acids research·2025
Same author

Women in Autophagy: an initiative to promote gender parity in science.

Nature cell biology·2024
Same author

Structure-activity relationship study of small-molecule inhibitor of Atg12-Atg3 protein-protein interaction.

Bioorganic & medicinal chemistry letters·2024
Same author

WIPI2b recruitment to phagophores and ATG16L1 binding are regulated by ULK1 phosphorylation.

EMBO reports·2024
Same author

Loss of EIF4G2 mediates aggressiveness in distinct human endometrial cancer subpopulations with poor survival outcome in patients.

Oncogene·2024
Same author

Loss-of-function cancer-linked mutations in the EIF4G2 non-canonical translation initiation factor.

Life science alliance·2023

Related Experiment Video

Updated: May 6, 2026

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

12.7K

The DAP-kinase interactome.

Shani Bialik1, Adi Kimchi

  • 1Department of Molecular Genetics, Weizmann Institute of Science, 76100, Rehovot, Israel.

Apoptosis : an International Journal on Programmed Cell Death
|November 14, 2013
PubMed
Summary

Death-associated protein kinase (DAPK) regulates cellular activities through its interactome. This review clarifies DAPK regulation and its diverse cellular effects, including apoptosis and cytoskeletal functions.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Death-associated protein kinase (DAPK) is a Ca(2+)/calmodulin-regulated kinase.
  • DAPK is involved in multiple cellular processes, including cell death, motility, and signaling cascades.
  • DAPK function is regulated by intramolecular signaling, protein interactions, and ubiquitin-dependent systems.

Purpose of the Study:

  • To review the DAPK interactome, encompassing its substrates, effectors, and regulators.
  • To elucidate the regulatory mechanisms governing DAPK activity.
  • To clarify how DAPK mediates its diverse cellular effects.

Main Methods:

  • Literature review of studies on DAPK substrates, interacting proteins, and regulatory pathways.
  • Analysis of DAPK's role in various cellular processes like apoptosis, autophagy, and necrosis.

More Related Videos

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

18.0K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

7.4K

Related Experiment Videos

Last Updated: May 6, 2026

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

12.7K
Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

18.0K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

7.4K
  • Examination of DAPK's catalytic-dependent and independent functions.
  • Main Results:

    • DAPK phosphorylates various kinases (e.g., ZIP-kinase, PKD) and proteins (e.g., Pin1, myosin II, tropomyosin).
    • DAPK mediates cytoskeletal functions, cell death pathways (apoptosis, autophagy, necrosis), and signaling.
    • DAPK also exhibits catalytic-independent functions, activating proteins like pyruvate kinase M2 and NLRP3.

    Conclusions:

    • The DAPK interactome network is crucial for understanding its regulation and cellular functions.
    • DAPK plays a multifaceted role in cellular physiology, impacting diverse pathways.
    • Further research is needed to establish the physiological significance of all identified DAPK substrates and interacting proteins.