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

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.5K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.2K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.2K
Phosphorylation01:02

Phosphorylation

50.3K
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...
50.3K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K

You might also read

Related Articles

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

Sort by
Same author

The functions and inhibitors of protein tyrosine phosphatase B from <i>Mycobacterium tuberculosis</i>.

Frontiers in immunology·2026
Same author

Palmitoylation of CLDN12 regulated by ZDHHC7 and APT1/2 promotes hepatitis C virus entry.

Journal of virology·2026
Same author

Analysis of imported Chikungunya cases in China from 2006 to 2026.

Frontiers in microbiology·2026
Same author

Pre-zoonotic adaptation of Andes virus before spillover: Implications for cross-host and human transmission.

The Journal of infection·2026
Same author

WPV1 resurgence and the dominant threat of cVDPV2: a 10-year global epidemiological analysis (2017-2026).

International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases·2026
Same author

Decoding the complex receptor landscape of enterovirus D68.

PLoS pathogens·2026
Same journal

Shared and context-specific mechanisms of T cell exhaustion in chronic viral infections and cancer: Transcriptional, metabolic, epigenetic, and therapeutic perspectives.

Cytokine & growth factor reviews·2026
Same journal

Temporal dynamics of type I interferon signaling in checkpoint inhibitor response and resistance.

Cytokine & growth factor reviews·2026
Same journal

The role of osteoprotegerin in colorectal cancer: Molecular interactions, mechanistic insights, and therapeutic implications.

Cytokine & growth factor reviews·2026
Same journal

Designing next-generation interleukin immunotherapy: A cytokine-guided framework for precision cancer therapy.

Cytokine & growth factor reviews·2026
Same journal

Fibroblast growth factor homologous factors in neural signaling: Molecular mechanisms and disease-relevant dysregulation.

Cytokine & growth factor reviews·2026
Same journal

Cytokine-mediated intrinsic and extrinsic regulation of anti-tumor adoptive T cell therapy.

Cytokine & growth factor reviews·2026
See all related articles

Related Experiment Video

Updated: Jul 1, 2025

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
16:33

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE

Published on: February 18, 2013

36.0K

When pyro(ptosis) meets palm(itoylation).

Lu Jiang1, Zirui Wang1, Ting Xu2

  • 1Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan, Shandong 250013, China; Department of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong 250117, China; Medical Science and Technology Innovation Center, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong 250117, China.

Cytokine & Growth Factor Reviews
|March 12, 2024
PubMed
Summary
This summary is machine-generated.

Protein palmitoylation regulates pyroptosis, a key immune process. This modification affects critical proteins like cGAS, NLRP3, STING, GSDMD, and NODs, influencing inflammation and cell death pathways.

Keywords:
GSDMDNLRP3cGASpalmitoylationpyroptosis

More Related Videos

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
07:27

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

Published on: April 9, 2021

5.2K
Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
08:28

Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins

Published on: March 29, 2020

6.7K

Related Experiment Videos

Last Updated: Jul 1, 2025

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
16:33

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE

Published on: February 18, 2013

36.0K
Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
07:27

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

Published on: April 9, 2021

5.2K
Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
08:28

Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins

Published on: March 29, 2020

6.7K

Area of Science:

  • Immunology
  • Molecular Biology
  • Cellular Biology

Background:

  • Pyroptosis is a crucial programmed cell death pathway involved in immune responses.
  • Protein palmitoylation, the addition of fatty acids to cysteine residues, is increasingly recognized as a key regulator of cellular processes.
  • Dysregulation of pyroptosis is implicated in various inflammatory diseases and infections.

Purpose of the Study:

  • To review the significant roles of protein palmitoylation in regulating key proteins involved in pyroptosis.
  • To elucidate the mechanisms by which palmitoylation influences pyroptosis-related protein function and downstream signaling.
  • To highlight the implications of palmitoylation in immune responses and inflammation.

Main Methods:

  • Literature review of recent studies on protein palmitoylation and pyroptosis.
  • Analysis of specific palmitoylation sites and their impact on protein function (e.g., cGAS, NLRP3, STING, GSDMD, NOD1/2).
  • Integration of findings to provide a comprehensive overview of palmitoylation's role in pyroptosis regulation.

Main Results:

  • Palmitoylation by specific ZDHHC enzymes regulates the activity and localization of cGAS, NLRP3, and STING.
  • Palmitoylation of GSDMD and GSDME is essential for pyroptosis execution, including pore formation and membrane translocation.
  • Palmitoylation of NOD1 and NOD2 influences their immune signaling pathways in response to bacterial stimuli.

Conclusions:

  • Protein palmitoylation is a critical post-translational modification that fine-tunes pyroptosis.
  • Understanding these palmitoylation events provides insights into immune regulation and potential therapeutic targets for inflammatory diseases.
  • Further research is needed to clarify conflicting findings, such as the role of ZDHHC5 in NLRP3 palmitoylation.