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

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,...
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...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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...

You might also read

Related Articles

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

Sort by
Same author

The cytoskeleton of pathogenic protists.

Bioscience reports·2026
Same author

Metal-metronidazole derivatives as potential antitrichomonal agents on Trichomonas vaginalis.

Experimental parasitology·2026
Same author

Breaking the ice - simplified freeze-fracture of parasitic protists: a cost-effective approach without highly specialised equipment.

Memorias do Instituto Oswaldo Cruz·2025
Same author

Looking Back to Move Forward: Tannic Acid in TEM of Parasitic Protozoa.

The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society·2025
Same author

Effects of cardanol-based phospholipid analogs on Trichomonas vaginalis.

Experimental parasitology·2024
Same author

Three-dimensional cellular architecture of the sigmoid filament in Trichomonas vaginalis.

Journal of structural biology·2024

Related Experiment Video

Updated: Jul 15, 2026

A Photodynamic Approach to Study Function of Intracellular Vesicle Rupture
05:16

A Photodynamic Approach to Study Function of Intracellular Vesicle Rupture

Published on: March 17, 2023

Golgi complex disassembly caused by light-activated calphostin C involves MAPK and PKA.

J A Morgado-Díaz1, G Montesano, S De Souza Fernandes

  • 1Grupo de Biologia Estrutural, Divisão de Biologia Celular, Centro de Pesquisas, Instituto Nacional de Câncer, Rio de Janeiro, RJ 20231-050, Brazil. jmorgado@inca.gov.br

Tissue & Cell
|April 7, 2007
PubMed
Summary

Light-activated Calphostin C causes Golgi complex disassembly in HT-29 cells. This process involves Mitogen-Activated Protein Kinase (MAPK) and Protein Kinase A (PKA), highlighting a novel regulatory mechanism.

More Related Videos

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

Related Experiment Videos

Last Updated: Jul 15, 2026

A Photodynamic Approach to Study Function of Intracellular Vesicle Rupture
05:16

A Photodynamic Approach to Study Function of Intracellular Vesicle Rupture

Published on: March 17, 2023

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Golgi complex is crucial for protein modification and transport.
  • Understanding cellular responses to external stimuli like light-activated compounds is vital.
  • The role of specific kinases in Golgi dynamics during drug treatment requires elucidation.

Purpose of the Study:

  • To investigate the involvement of MAPK and PKA in Calphostin C-induced Golgi complex disassembly.
  • To explore the impact of Calphostin C on the endocytic pathway.
  • To identify the signaling pathways regulating Golgi breakdown.

Main Methods:

  • Immunofluorescence microscopy to assess Golgi fragmentation.
  • Electron microscopy to analyze ultrastructural changes in the Golgi.
  • Treatment with Calphostin C and specific kinase inhibitors (PD98059 for MAPK, H-89 for PKA).

Main Results:

  • Calphostin C induced Golgi complex fragmentation and dispersal, forming vesicle clusters and tubule-vesicular structures.
  • Calphostin C treatment inhibited the endocytic pathway.
  • Pretreatment with MAPK and PKA inhibitors (PD98059 and H-89) blocked Calphostin C-induced Golgi disassembly and endocytic inhibition.

Conclusions:

  • MAPK and PKA play a critical role in the Golgi complex disassembly induced by light-activated Calphostin C.
  • A novel mechanism involving MAPK and PKA in regulating Golgi breakdown by Calphostin C in HT-29 cells is proposed.
  • Calphostin C affects both Golgi structure and endocytic function through kinase-dependent pathways.