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

Bacterial Phylum Chlamydiae01:29

Bacterial Phylum Chlamydiae

The phylum Chlamydiae or Chlamydiota is composed of a single order, Chlamydiales. This phylum consists entirely of obligate intracellular parasites that infect eukaryotic hosts. While human pathogens within this group have been studied extensively, the phylum encompasses many species capable of interacting with various eukaryotic organisms. Members of Chlamydiae are typically small cocci, approximately 0.5 μm in diameter, and exhibit a distinctive developmental cycle. As is characteristic of...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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,...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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...
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,...
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...

You might also read

Related Articles

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

Sort by
Same author

A metabolic constraint in de novo NAD+ synthesis drives mucosal inflammation in IBD.

Journal of Crohn's & colitis·2026
Same author

Autophagy selectively clears ER in TNF-α-induced muscle atrophy.

Autophagy reports·2026
Same author

Corrigendum to "Enhanced LRP8 expression induced by Helicobacter pylori drives gastric cancer progression by facilitating β-Catenin nuclear translocation". [J. Adv. Res. 69 (2025) 299-312].

Journal of advanced research·2025
Same author

Cross-platform clinical proteomics using the Charité open standard for plasma proteomics (OSPP).

Nature communications·2025
Same author

Neuromuscular dysfunction in patient-derived FUS<sup>R244RR</sup>-ALS iPSC model via axonal downregulation of neuromuscular junction proteins.

NAR molecular medicine·2025
Same author

ERV3-MLT1 provides cis-regulatory elements for human placental functioning and are commonly dysregulated in human-specific preeclampsia.

Genome biology·2025

Related Experiment Video

Updated: Jun 27, 2026

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis
10:32

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

Published on: June 10, 2020

Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation.

Adrian Mehlitz1, Sebastian Banhart, Simone Hess

  • 1Department of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany.

FEMS Microbiology Letters
|November 20, 2008
PubMed
Summary

Chlamydia trachomatis effector Tarp is phosphorylated by multiple kinases, including Src, Abl, and Syk. This promiscuous phosphorylation by Syk, Abl, and Src kinases does not impede bacterial inclusion formation.

More Related Videos

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis
10:35

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis

Published on: January 30, 2020

Forward Genetic Approaches in Chlamydia trachomatis
09:03

Forward Genetic Approaches in Chlamydia trachomatis

Published on: October 23, 2013

Related Experiment Videos

Last Updated: Jun 27, 2026

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis
10:32

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

Published on: June 10, 2020

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis
10:35

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis

Published on: January 30, 2020

Forward Genetic Approaches in Chlamydia trachomatis
09:03

Forward Genetic Approaches in Chlamydia trachomatis

Published on: October 23, 2013

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Chlamydia trachomatis is an obligate intracellular bacterium that manipulates host cells for survival and replication.
  • The effector protein Tarp (translocated actin-recruiting phosphoprotein) is translocated into the host cytoplasm and rapidly tyrosine phosphorylated.
  • Abl and Src kinases were previously implicated in Tarp phosphorylation, but the full kinase network remained unclear.

Purpose of the Study:

  • To comprehensively investigate the host kinases responsible for tyrosine phosphorylation of Chlamydia trachomatis Tarp.
  • To determine the functional significance of Tarp phosphorylation in the context of bacterial infection.

Main Methods:

  • Utilized chemical inhibition of Src family kinases (SFKs) and Abl kinase.
  • Employed Src, Yes, Fyn (SYF)-deficient cells to assess the role of SFKs.
  • Tested the in vitro kinase activity of Syk, Btk, and Jak2 against Tarp.
  • Inhibited Syk in an SYF background to evaluate combined kinase inhibition effects.
  • Monitored Chlamydia inclusion formation as a measure of infection progression.

Main Results:

  • Chemical inhibition of SFKs partially reduced Tarp phosphorylation.
  • Tarp phosphorylation was dampened but not completely blocked in SYF-deficient cells.
  • Inhibition of Abl in SYF-deficient cells still resulted in incomplete Tarp phosphorylation.
  • Spleen tyrosine kinase (Syk) was identified as a potent kinase for Tarp in vitro.
  • Combined inhibition of SFKs and Syk significantly reduced Tarp phosphorylation.
  • Despite extensive kinase inhibition, Chlamydia inclusion formation remained unaffected.

Conclusions:

  • Tarp is a promiscuous substrate phosphorylated by a complex network of host kinases, including Syk, Abl, and SFKs.
  • The identified kinases (Syk, Abl, SFKs) contribute to Tarp phosphorylation during Chlamydia trachomatis infection.
  • Tarp phosphorylation by these kinases is not essential for bacterial inclusion formation, suggesting alternative regulatory mechanisms or roles.