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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...

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Related Experiment Video

Updated: Jun 12, 2026

Presynapse Formation Assay Using Presynapse Organizer Beads and &ldquo;Neuron Ball&rdquo; Culture
10:17

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Are presynaptic proteins predisposed to self-assemble?

Ann Y N Goldstein1, Thomas L Schwarz

  • 1FM Kirby Neurobiology Center of Children's Hospital, Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.

Neuron
|June 16, 2010
PubMed
Summary
This summary is machine-generated.

ARL-8 GTPase regulates presynaptic assembly by preventing material aggregation. This discovery offers new insights into how neurons form precise connections during development.

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

Related Experiment Videos

Last Updated: Jun 12, 2026

Presynapse Formation Assay Using Presynapse Organizer Beads and &ldquo;Neuron Ball&rdquo; Culture
10:17

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Synapse formation is crucial for neuronal connectivity.
  • Precise regulation of presynaptic assembly is essential for targeting accuracy.

Discussion:

  • ARL-8 GTPase identified as a key regulator of presynaptic assembly.
  • ARL-8 prevents aggregation of presynaptic material during transport.
  • Suggests ARL-8 functions as a dispersant to inhibit premature synaptic formation.

Key Insights:

  • ARL-8 GTPase controls the transport and localization of presynaptic components.
  • Loss of ARL-8 function leads to aberrant aggregation of synaptic vesicles.
  • ARL-8 is critical for ensuring proper targeting of presynaptic machinery.

Outlook:

  • Further research into ARL-8's mechanism could reveal therapeutic targets for neurological disorders.
  • Understanding ARL-8 function may elucidate mechanisms of synaptic plasticity.
  • Potential for ARL-8 as a target for modulating synapse formation in developmental contexts.