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Related Concept Videos

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
COP Coated Vesicles00:59

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)00:53

Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)

Acyclic diene metathesis polymerization or ADMET polymerization involves cross-metathesis of terminal dienes, such as 1,8-nonadiene, to give linear unsaturated polymer and ethylene. As ADMET is a reversible process, the formed ethylene gas must be removed from the reaction mixture to complete the polymerization process.
Similar to cross-metathesis, ADMET also involves the formation of metallacyclobutane intermediate by [2+2] cycloaddition of one of the double bonds of a terminal diene with...
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.
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...

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Related Experiment Video

Updated: May 19, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Cargo-Adaptor Cooperation Programs Retromer Coat Architecture.

Marta Pardo-Piñón1,2, Raffaele Coray1,2, Pengwei Zhang3,4

  • 1Instituto Biofisika (UPV/EHU, CSIC), University of the Basque Country, Leioa, Spain.

Biorxiv : the Preprint Server for Biology
|May 18, 2026
PubMed
Summary
This summary is machine-generated.

Sorting nexin 12 (SNX12) acts as a retromer adaptor for human papillomavirus 16 (HPV16) infection. This interaction shapes retromer coat architecture, demonstrating how cargo and adaptors program cellular transport carriers.

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Last Updated: May 19, 2026

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Published on: July 10, 2019

Area of Science:

  • Cell Biology
  • Virology
  • Structural Biology

Background:

  • Retromer complexes, with sorting nexin (SNX) adaptors, mediate endosomal cargo retrieval.
  • The precise mechanisms by which adaptor-cargo interactions dictate retromer coat structure are not fully understood.

Purpose of the Study:

  • To identify the specific retromer adaptor involved in human papillomavirus 16 (HPV16) infection.
  • To elucidate how adaptor-cargo binding influences retromer coat assembly and membrane tubulation.

Main Methods:

  • Identification of sorting nexin 12 (SNX12) as the key retromer adaptor for HPV16.
  • Structural analysis using X-ray crystallography to determine cargo recognition modes.
  • Cryo-electron tomography to visualize reconstituted retromer assemblies and their lattice configurations.

Main Results:

  • SNX12 is essential for HPV16 infection, with the viral L2 capsid protein tail directly interacting with SNX12-retromer complexes.
  • Crystal structure reveals a conserved mechanism for cargo recognition by the adaptor.
  • Cryo-electron tomography shows retromer arches forming distinct lattice structures (multi-start helices) stabilized by membrane-proximal interfaces, accommodating membrane curvature via hinge-like motions.

Conclusions:

  • Cargo and adaptor identity are critical determinants of retromer coat architecture.
  • Retromer functions as a programmable system capable of generating specific transport carriers for distinct cellular routes.
  • These findings provide insights into viral hijacking of cellular machinery and the fundamental principles of vesicular transport.