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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Cell Motility through Blebbing01:16

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Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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...
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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Related Experiment Video

Updated: Nov 15, 2025

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
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Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

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Structural insights into membrane remodeling by SNX1.

Yan Zhang1, Xiaoyun Pang2, Jian Li3

  • 1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Proceedings of the National Academy of Sciences of the United States of America
|March 4, 2021
PubMed
Summary

Sorting nexin 1 (SNX1) proteins form helical lattices around tubular membranes, deforming them to create transport carriers. This structural insight clarifies SNX1

Keywords:
SNX1coat complexcryoelectron microscopyhelical reconstructionmembrane deformation

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Sorting nexins (SNX) are crucial proteins involved in membrane trafficking.
  • SNX proteins facilitate the formation of transport carriers within endosomal pathways.
  • Understanding SNX protein function requires detailed structural and mechanistic insights.

Purpose of the Study:

  • To elucidate the mechanism by which the sorting nexin SNX1 deforms membranes.
  • To determine the structural basis of SNX1 assembly and its role in carrier generation.
  • To compare SNX1 structure with retromer-SNX coat complexes and understand assembly dynamics.

Main Methods:

  • Cryoelectron microscopy was employed to visualize SNX1 structures.
  • Detailed structural analysis of SNX1 assemblies on tubular membranes.
  • Comparative structural analysis of SNX1 and retromer-SNX complexes.

Main Results:

  • SNX1 assembles into a crosslinked lattice of helical rows of dimers around tubular membranes.
  • The structure reveals how SNX1 domains contribute to membrane deformation.
  • Comparison with retromer-SNX complexes highlights retromer's influence on SNX organization and suggests assembly intermediates.

Conclusions:

  • SNX1's helical lattice structure is key to its membrane-deforming capability.
  • Structural insights into SNX1 provide a molecular basis for its role in endosomal transport.
  • Understanding SNX1-retromer interactions offers clues into the assembly of coat complexes for membrane trafficking.