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Related Concept Videos

Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...
Regulation of Nuclear Protein Sorting01:45

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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

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Related Experiment Video

Updated: Jul 9, 2026

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
12:43

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE

Published on: July 29, 2014

RIN4 fragments released by AvrRpt2 promote NDR1-dependent activation of RPS2.

Ahmed J Afzal1,2,3, Maheen Alam1,4, Jianhua Huang4,5

  • 1Department of Horticulture and Crop Science, Columbus, OH 43210, USA.

The Plant Cell
|July 7, 2026
PubMed
Summary
This summary is machine-generated.

Plant immune receptors like Resistance to Pseudomonas syringae2 (RPS2) are activated by pathogen effectors. This study reveals how RIN4 cleavage products regulate RPS2 activation, involving the defense protein NDR1.

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Last Updated: Jul 9, 2026

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
12:43

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Published on: July 29, 2014

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Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Area of Science:

  • Plant immunity
  • Molecular plant-pathogen interactions
  • Plant cell signaling

Background:

  • Plant nucleotide-binding, leucine-rich-repeat (NLR) immune receptors, such as Resistance to Pseudomonas syringae2 (RPS2), are crucial for recognizing pathogen effectors and initiating defense responses.
  • The Pseudomonas effector AvrRpt2 cleaves the host protein RPM1-interacting protein 4 (RIN4), which is linked to RPS2 activation and pathogen virulence.

Purpose of the Study:

  • To elucidate the precise mechanisms by which RIN4 cleavage products modulate RPS2 activation.
  • To investigate the role of the defense signaling protein NON-RACE-SPECIFIC DISEASE RESISTANCE 1 (NDR1) in AvrRpt2-induced RPS2 activation.

Main Methods:

  • Analysis of RPS2 activation by different RIN4 derivatives in planta.
  • Investigating the requirement of NDR1 for RPS2 activation by AvrRpt2 and RIN4 derivatives.
  • Characterization of the functional roles of RIN4 cleavage fragments in RPS2 signaling.

Main Results:

  • Non-membrane-tethered RIN4 derivatives act as potent cytosolic activators of RPS2.
  • Activation of RPS2 by these RIN4 derivatives and by AvrRpt2 requires NDR1.
  • RIN4 C-terminal fragments suppress RPS2, while internal fragments overcome this suppression, demonstrating contrasting roles of cleavage products.

Conclusions:

  • RPS2 activation by AvrRpt2 is a complex process involving specific RIN4 cleavage products and the NDR1 signaling pathway.
  • The interplay between RIN4 fragments dictates the outcome of RPS2 activation, highlighting a sophisticated regulatory mechanism in plant immunity.