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

MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such asĀ  SH2...
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

You might also read

Related Articles

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

Sort by
Same author

Single-cell and Spatial Transcriptomic Profiling Reveal that LAPTM5-mediated Ferroptosis in Macrophages Induces Fibroblast Dysfunction and Amplifies Periodontal Inflammation.

InflammationĀ·2026
Same author

PBAE nanoparticle-mediated delivery of ASCL1 and NGN2 genes for astroglia-to-neuron reprogramming to remodel glial scar for spinal cord injury repair.

Stem cell research & therapyĀ·2026
Same author

Novel Transcatheter Edge-to-Edge Repair System for High-Risk Primary Mitral Regurgitation: 2-Year Pivotal Trial Outcomes.

JACC. AsiaĀ·2026
Same author

PDZD8 overexpression alleviates early brain injury via regulating MERCs integrity after experimental subarachnoid hemorrhage.

Journal of neuroinflammationĀ·2026
Same author

Spatial multi-omics implicate the interaction between Tpex and B cells in tertiary lymphoid structures after neoadjuvant therapy.

Cancer discoveryĀ·2026
Same author

The perioperative effect of ERAS protocol in patients with lung cancer: a randomized controlled study.

Journal of cardiothoracic surgeryĀ·2026
Same journal

SMURF1-mediated EFEMP1 ubiquitination reverses the resistance of HCC cells to sorafenib by promoting ferroptosis.

Biochemical and biophysical research communicationsĀ·2026
Same journal

Development and validation of HSP90AA1 as a risk gene in a HIF-1Ī± pathway-related prognostic signature for hepatocellular carcinoma.

Biochemical and biophysical research communicationsĀ·2026
Same journal

Quercetin suppresses TGF-Ī²1-induced proliferation and migration of vascular smooth muscle cells via the Smad2/3/MMP-9 signaling axis.

Biochemical and biophysical research communicationsĀ·2026
Same journal

Biosynthesis, characterization and biological potential of microbe-mediated silver nanoparticles using thermophilic actinomycetes, Streptomyces nigra.

Biochemical and biophysical research communicationsĀ·2026
Same journal

COP9 signalosome 8 mediated autophagy drives proliferation, invasion, and metastasis in pancreatic ductal adenocarcinoma.

Biochemical and biophysical research communicationsĀ·2026
Same journal

Tumor budding in colorectal cancer: partial EMT, microenvironmental remodeling, and metastatic competence.

Biochemical and biophysical research communicationsĀ·2026
See all related articles

Related Experiment Video

Updated: May 20, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Stress-induced interaction between p38 MAPK and HSP70.

Xiaowei Gong1, Tingting Luo, Peng Deng

  • 1Department of Pathophysiology and Key Laboratory of Proteomics of Guangdong Province, Southern Medical University, Guangzhou 510515, China. gongxw@fimmu.com

Biochemical and Biophysical Research Communications
|July 31, 2012
PubMed
Summary
This summary is machine-generated.

Heat shock protein 70 (HSP70) may act as a chaperone for p38 mitogen-activated protein kinase (MAPK) nuclear translocation. This interaction is stress-induced and affects downstream signaling, suggesting a novel role for HSP70 in p38 MAPK pathways.

More Related Videos

Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Related Experiment Videos

Last Updated: May 20, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Stress response mechanisms

Background:

  • p38 MAPK is crucial in cellular responses to stress and inflammation.
  • Understanding p38 MAPK activation and nuclear translocation is vital for comprehending its biological roles.
  • The precise mechanisms governing p38 MAPK nuclear import remain incompletely understood.

Purpose of the Study:

  • To investigate the potential chaperone proteins involved in p38 MAPK nuclear translocation.
  • To identify and characterize the interaction between p38 MAPK and its potential chaperone.
  • To elucidate the functional significance of this interaction in cellular stress responses.

Main Methods:

  • Endogenous pull-down assays to identify interacting proteins.
  • In vitro and in vivo confirmation of protein-protein interactions.
  • Identification of specific interaction domains between p38 MAPK and HSP70.
  • Analysis of stress-induced co-localization within the nucleus.
  • Assessment of HSP70's effect on downstream p38 MAPK signaling (MK2 phosphorylation).

Main Results:

  • Heat shock protein 70 (HSP70) was identified as a potential interacting protein of p38 MAPK.
  • The interaction between p38 MAPK and HSP70 was confirmed both in vitro and in vivo.
  • Specific interaction domains were mapped for the p38 MAPK-HSP70 complex.
  • Stress stimuli induced the nuclear co-localization of p38 MAPK and HSP70.
  • HSP70 was found to be related to the phosphorylation of MK2, a downstream target of p38 MAPK.

Conclusions:

  • HSP70 interacts with p38 MAPK and facilitates its stress-induced nuclear translocation.
  • This interaction suggests HSP70 functions as a chaperone for p38 MAPK nuclear import.
  • The findings provide new insights into the regulation of p38 MAPK signaling pathways.
  • HSP70's role in p38 MAPK translocation has implications for understanding cellular stress responses and inflammatory processes.