Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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....

The JAK-STAT Signaling Pathway

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...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Protein Modifications in the RER

Protein Modifications in the RER

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...

Phosphoinositides and PIPs

Phosphoinositides and PIPs

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...

Lipids as Anchors

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...

You might also read

Related Articles

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

Sort by

Same author

SARS-CoV-2 Delta variant re-emerges in US farmed mink and free-ranging white-tailed deer in 2022-2023.

Nature communications·2026

Same author

Gene duplication and retrotransposition diversify the antiviral repertoire of macaque IFITM proteins.

bioRxiv : the preprint server for biology·2026

Same author

Genetic and pharmacological inactivation of peptidoglycan remodeling increases antibiotic susceptibility of vancomycin-resistant Enterococcus faecium.

Nature communications·2026

Same author

Genetic and pharmacological inactivation of peptidoglycan remodeling increases antibiotic susceptibility of vancomycin-resistant <i>Enterococcus faecium</i>.

bioRxiv : the preprint server for biology·2026

Same author

Influenza virus hitches a cellular ride to the heart.

Cell host & microbe·2026

Same author

Discovery and Development of Antibacterial Peptidoglycan Hydrolase Inhibitors.

ACS infectious diseases·2026

Search research articles

Related Experiment Video

Updated: Nov 15, 2025

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Protein S-palmitoylation in immunity.

Tandrila Das¹, Jacob S Yount², Howard C Hang^1,3

¹Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, USA.

|March 3, 2021

Summary

S-palmitoylation, a protein lipid modification, regulates immune cell functions. Understanding this process offers new therapeutic strategies for immune response modulation.

Keywords:

S-palmitoylation adaptive immunity innate immune effectors innate immune receptors

More Related Videos

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

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

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

Published on: February 18, 2013

Related Experiment Videos

Last Updated: Nov 15, 2025

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

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

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

Published on: February 18, 2013

Area of Science:

Biochemistry
Immunology
Cell Biology

Background:

S-palmitoylation is a reversible posttranslational lipid modification crucial for protein function.
This modification impacts protein activity, stability, trafficking, and interactions.
Numerous S-palmitoylated proteins are involved in immunity.

Purpose of the Study:

To review S-palmitoylated immune receptors and effectors.
To discuss the dynamic regulation of these proteins at cellular membranes.
To explore therapeutic potential for modulating immune responses via S-palmitoylation.

Main Methods:

Global profiling of immune cells.
Targeted analysis of S-palmitoylated proteins.
Literature review of S-palmitoylation in immune regulation.

Main Results:

Identification of many S-palmitoylated immunity-associated proteins.
Insights into the dynamic regulation of these proteins at the cell membrane.
Understanding the role of S-palmitoylation in immune response specificity and balance.

Conclusions:

S-palmitoylation is a key regulator of immune cell function.
Targeting S-palmitoylation pathways presents therapeutic opportunities for immune disorders.