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Related Concept Videos

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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...
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Golgi Matrix Proteins01:12

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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.
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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.
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Related Experiment Video

Updated: Oct 8, 2025

Studying Organelle Dynamics in B Cells During Immune Synapse Formation
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Revisiting I-BAR Proteins at Central Synapses.

Christina Chatzi1, Gary L Westbrook1

  • 1Vollum Institute, Oregon Health and Science University, Portland, OR, United States.

Frontiers in Neural Circuits
|January 3, 2022
PubMed
Summary

Inverse BAR (I-BAR) proteins regulate dendritic spine shape and function, crucial for synaptic plasticity and memory. Their interactions influence neural network rewiring in the central nervous system (CNS).

Keywords:
BAR domain proteindendritic spinesfilopodiamembrane curvaturepost-synapticsynaptic plasticity

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Quantifying Synapses: an Immunocytochemistry-based Assay to Quantify Synapse Number
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Dendritic spines are key postsynaptic structures in the CNS, vital for synaptic efficacy, plasticity, learning, and memory.
  • Spine dynamics, including shape, number, and molecular composition, are regulated by neural activity.
  • Spine formation involves membrane protrusions, a process less studied than in non-neuronal cells.

Purpose of the Study:

  • To review the role of BAR domain proteins, specifically inverse BAR (I-BAR) proteins, in dendritic spine formation and function.
  • To highlight three CNS-expressed I-BAR proteins (Mtss2, MIM, IRSp53) and their distinct roles in synapse formation and plasticity.
  • To discuss how I-BAR protein interactions and signaling platforms contribute to neural circuit function.

Main Methods:

  • Literature review focusing on BAR domain proteins and their function in the CNS.
  • Analysis of studies on I-BAR proteins (Mtss2, MIM, IRSp53) and their impact on membrane curvature.
  • Examination of protein-protein interactions, including heterooligomerization, and signaling crosstalk.

Main Results:

  • I-BAR proteins sense and induce outward membrane curvature, bridging the cell membrane and cytoskeleton.
  • Mtss2, MIM, and IRSp53 promote negative, concave curvature and have distinct functions in synapse formation and plasticity.
  • I-BAR protein activity is modulated by signaling crosstalk and heterooligomerization, forming dynamic signaling platforms.

Conclusions:

  • I-BAR proteins are critical regulators of dendritic spine morphology and function.
  • Understanding I-BAR protein spatiotemporal expression and interactions offers insights into activity-dependent neural plasticity and network rewiring.
  • These proteins represent key players in the interplay between synaptic plasticity and CNS network organization.