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

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

9.3K
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...
9.3K
Autophagy01:27

Autophagy

4.6K
Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
4.6K
Autophagic Cell Death01:18

Autophagic Cell Death

3.6K
Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
3.6K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.6K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.6K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

12.5K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
12.5K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.7K
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...
8.7K

You might also read

Related Articles

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

Sort by
Same author

Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochondrial tubulation and fission.

Nature communications·2025
Same author

Mitochondrial YME1L1 governs unoccupied protein translocase channels.

Nature cell biology·2025
Same author

STING induces HOIP-mediated synthesis of M1 ubiquitin chains to stimulate NF-κB signaling.

The EMBO journal·2024
Same author

INF2-mediated actin polymerization at ER-organelle contacts regulates organelle size and movement.

bioRxiv : the preprint server for biology·2024
Same author

STING induces HOIP-mediated synthesis of M1 ubiquitin chains to stimulate NFκB signaling.

bioRxiv : the preprint server for biology·2023
Same author

Nix interacts with WIPI2 to induce mitophagy.

The EMBO journal·2023
Same journal

A human-specific genetic modifier reconfigures large-scale cortical network dynamics underlying behavioral performance.

bioRxiv : the preprint server for biology·2026
Same journal

<i>Staphylococcus aureus</i> uses a eukaryotic-like uridyltransferase to make UDP-GlcNAc for cell wall synthesis.

bioRxiv : the preprint server for biology·2026
Same journal

Dynamic redistribution of eIF4F controls cap-dependent translation initiation.

bioRxiv : the preprint server for biology·2026
Same journal

When does additional information improve accuracy of RNA secondary structure prediction?

bioRxiv : the preprint server for biology·2026
Same journal

Normative brain-state trajectories reveal deviation from healthy aging in Alzheimer's disease.

bioRxiv : the preprint server for biology·2026
Same journal

Noradrenergic infraslow rhythm during sleep is the critical link between heart-rate dynamics and memory consolidation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Sep 18, 2025

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
09:10

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells

Published on: October 28, 2019

7.4K

TNIP1 and Autophagy Receptors regulate STING Signaling.

Eric N Bunker1, Tara D Fischer1, Peng-Peng Zhu1

  • 1Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health; Bethesda, MD, USA.

Biorxiv : the Preprint Server for Biology
|June 26, 2025
PubMed
Summary
This summary is machine-generated.

Autophagy receptors and TNIP1 bind to STING-associated vesicles, regulating innate immunity. TNIP1 negatively controls STING-mediated NF-κB and Interferon signaling independently of autophagy.

Keywords:
ATG8CASMHOIPInterferonNFkBUbiquitincGAS

More Related Videos

The Lactate Dehydrogenase Sequestration Assay &#8212; A Simple and Reliable Method to Determine Bulk Autophagic Sequestration Activity in Mammalian Cells
09:34

The Lactate Dehydrogenase Sequestration Assay — A Simple and Reliable Method to Determine Bulk Autophagic Sequestration Activity in Mammalian Cells

Published on: July 27, 2018

18.2K
Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.2K

Related Experiment Videos

Last Updated: Sep 18, 2025

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
09:10

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells

Published on: October 28, 2019

7.4K
The Lactate Dehydrogenase Sequestration Assay &#8212; A Simple and Reliable Method to Determine Bulk Autophagic Sequestration Activity in Mammalian Cells
09:34

The Lactate Dehydrogenase Sequestration Assay — A Simple and Reliable Method to Determine Bulk Autophagic Sequestration Activity in Mammalian Cells

Published on: July 27, 2018

18.2K
Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.2K

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • The cGAS-STING pathway triggers innate immune responses, involving LC3B lipidation and ubiquitylation on Golgi-related vesicles.
  • Mechanisms of Golgi-localized polyubiquitin chain regulation in immune signaling remain unclear, despite associations with NF-κB signaling.

Purpose of the Study:

  • To investigate the roles of ubiquitin- and LC3B-binding proteins in STING-mediated immune signaling.
  • To elucidate the mechanisms by which these proteins regulate STING-associated vesicles and downstream signaling pathways.

Main Methods:

  • Investigated the association of TNIP1 and autophagy receptors (p62, NBR1, NDP52, TAX1BP1, OPTN) with STING-induced vesicles.
  • Assessed the role of TBK1 kinase activity in vesicle recruitment and sequestration.
  • Determined the importance of specific protein domains (ubiquitin binding domains, LC3B-interacting regions) for recruitment.
  • Evaluated the functional impact of TNIP1 and OPTN on STING-mediated NF-κB and Interferon signaling.

Main Results:

  • TNIP1 and autophagy receptors associate with STING-induced Ub/LC3B-labeled vesicles.
  • p62 and NBR1 redundantly cluster these vesicles in the perinuclear region.
  • TBK1 kinase activity is not required for TNIP1/receptor recruitment but aids vesicle sequestration.
  • TNIP1 and OPTN's ubiquitin binding domains are crucial for recruitment; OPTN also uses a TBK1-dependent mechanism.
  • TNIP1 acts as a negative regulator of STING-mediated NF-κB and Interferon signaling.

Conclusions:

  • Autophagy receptors and TNIP1 participate in STING-mediated immune signaling through autophagy-independent mechanisms.
  • TNIP1 plays a significant role in negatively regulating STING-induced NF-κB and Interferon responses.
  • These findings reveal novel roles for autophagy-associated proteins in modulating STING immunity.