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

50.1K
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...
50.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.8K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.1K
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...
13.1K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

8.4K
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...
8.4K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
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,...
5.1K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

3.4K
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...
3.4K

You might also read

Related Articles

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

Sort by
Same author

Avoidance of MAIT cells is an essential determinant of <i>Listeria</i> monocytogenes pathogenesis.

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

Host methylglyoxal activates the <i>Listeria</i> virulence program, allowing bacteria to evade inflammatory phagocytes by cell-to-cell spread.

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

Reprogramming <i>Listeria monocytogenes</i> flavin metabolism to improve its therapeutic safety profile and broaden innate T-cell activation.

mBio·2025
Same author

MAIT cells induced by engineered <i>Listeria</i> exhibit antibacterial and antitumor activity.

bioRxiv : the preprint server for biology·2025
Same author

<i>Listeria monocytogenes</i> adenosine auxotrophs are impaired for intracellular and extracellular growth but retain potent immunogenicity.

Infection and immunity·2025
Same author

Stress-dependent activation of the <i>Listeria monocytogenes</i> virulence program ensures bacterial resilience during infection.

mBio·2025

Related Experiment Video

Updated: Jun 13, 2025

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress
08:39

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress

Published on: October 11, 2024

1.5K

Phosphorylation State Dictates Bacterial Stressosome Assembly and Function.

Allison Williams1, Elizabeth Martinez-Bond1, Ivanna Lopez-Ayala2

  • 1Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.

Research Square
|June 12, 2025
PubMed
Summary
This summary is machine-generated.

Bacterial stressosomes, crucial for survival, are regulated by protein phosphorylation. This study reveals how specific phosphorylation sites control stressosome structure, activation, and bacterial virulence, offering new antimicrobial targets.

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.4K
Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
10:59

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling

Published on: May 19, 2014

18.3K

Related Experiment Videos

Last Updated: Jun 13, 2025

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress
08:39

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress

Published on: October 11, 2024

1.5K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.4K
Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
10:59

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling

Published on: May 19, 2014

18.3K

Area of Science:

  • Bacterial pathogenesis
  • Molecular microbiology
  • Structural biology

Background:

  • Bacteria utilize stressosomes, large protein complexes, to sense and respond to environmental stressors.
  • The stressosome regulates the general stress response pathway, essential for bacterial survival and virulence.
  • Understanding stressosome regulation is key to developing novel antimicrobial strategies.

Purpose of the Study:

  • To elucidate the atomic structure of Listeria monocytogenes stressosomes.
  • To determine the role of protein phosphorylation in stressosome assembly, activation, and function.
  • To investigate the link between stressosome regulation, bacterial adaptation, and pathogenesis.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine stressosome structures.
  • Site-directed mutagenesis to create phosphomimetic and phosphodeficient mutants.
  • Functional assays including oxidative stress resistance and host cell virulence models.

Main Results:

  • Atomic structures of five Listeria monocytogenes stressosomes were solved, revealing inactive and activated states.
  • Phosphorylation at specific RsbR (T175, T209) and RsbS (S56) residues dictates stressosome assembly, stoichiometry, and activation dynamics.
  • Phosphorylation at T175 primes activation, S56 triggers RsbT release, and T209 fine-tunes the response intensity.
  • Mutants mimicking phosphorylation (T209E, S56D) enhanced stress resistance but reduced virulence.
  • Mutants lacking phosphorylation (T175A, S56A) were stress-sensitive but retained virulence.

Conclusions:

  • Phosphorylation acts as a critical regulatory switch controlling bacterial stressosome structure and function.
  • Structural dynamics of the stressosome directly impact bacterial adaptation and virulence.
  • Targeting stressosome phosphorylation offers a promising avenue for developing new antimicrobials against bacterial pathogens.