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

PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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 rapamycin-insensitive companion...
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 as  SH2...
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...
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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,...

You might also read

Related Articles

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

Sort by
Same author

Simultaneous Laparoscopic Repair of Iatrogenic Lumbar and Inguinal Hernias Using Combined TAPP and IPOM: A Case Report.

The Tokai journal of experimental and clinical medicine·2026
Same author

Outpatient visit intervals in chronic kidney disease: adherence to Kidney Disease: Improving Global Outcomes recommendations and determinants of variation.

Kidney research and clinical practice·2026
Same author

Microbial fermentation as a strategy for the abatement of peanut allergens.

Applied and environmental microbiology·2026
Same author

Treatment Outcomes of Durvalumab Combination Therapy in Patients with Biliary Tract Cancer.

The Tokai journal of experimental and clinical medicine·2026
Same author

Beyond Annual Averages: Rethinking Metrics For Emergency Department Crowding And Capacity Planning.

The Journal of emergency medicine·2025
Same author

A Case of Grade 3 Gastric Neuroendocrine Tumor with Glandular Formation: Diagnostic Process and Differentiation from Gastric Mixed Neuroendocrine-Non-Neuroendocrine Neoplasm.

Journal of Nippon Medical School = Nippon Ika Daigaku zasshi·2025

Related Experiment Video

Updated: Jul 14, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Physical and functional interaction between mortalin and Mps1 kinase.

Masayuki Kanai1, Zhiyong Ma, Hideki Izumi

  • 1Department of Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|June 19, 2007
PubMed
Summary

Mortalin (Hsp70 chaperone) interacts with Mps1 kinase, leading to mortalin phosphorylation and Mps1 super-activation. This interaction is crucial for mortalin

More Related Videos

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death
09:18

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Published on: December 27, 2016

Related Experiment Videos

Last Updated: Jul 14, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death
09:18

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Published on: December 27, 2016

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Mortalin, a member of the Hsp70 chaperone family, participates in diverse cellular processes.
  • Mps1 kinase is known to regulate centrosome duplication and the mitotic checkpoint.
  • Mortalin's role in centrosome duplication and its centrosomal localization have been previously suggested.

Purpose of the Study:

  • To identify kinases that physically interact with mortalin.
  • To elucidate the functional consequences of the mortalin-Mps1 interaction.
  • To investigate the role of Mps1 in mortalin's centrosomal localization and function.

Main Methods:

  • Identification of mortalin-interacting kinases.
  • Analysis of mortalin phosphorylation by Mps1 at specific residues (Thr62 and Ser65).
  • Assessment of Mps1 activity modulation by phosphorylated mortalin.
  • Investigation of mortalin's centrosomal localization in the presence and absence of Mps1.
  • Evaluation of Mps1-driven centrosome duplication acceleration with and without mortalin.

Main Results:

  • Mps1 was identified as a kinase that physically interacts with mortalin.
  • Mps1 phosphorylates mortalin on Thr62 and Ser65, which in turn super-activates Mps1.
  • Centrosomal localization of mortalin is dependent on the presence of Mps1.
  • Mps1-accelerated centrosome duplication requires both mortalin and its Mps1-mediated phosphorylation.

Conclusions:

  • Mortalin and Mps1 form a regulatory feedback loop where Mps1 phosphorylates mortalin, leading to Mps1 super-activation.
  • Mps1 is essential for the centrosomal localization of mortalin.
  • The mortalin-Mps1 interaction, including mortalin phosphorylation, plays a critical role in regulating centrosome duplication.