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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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...
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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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Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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...
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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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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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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Related Experiment Video

Updated: Oct 27, 2025

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

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Specific KIF1A-adaptor interactions control selective cargo recognition.

Jessica J A Hummel1, Casper C Hoogenraad1,2

  • 1Cell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Utrecht, the Netherlands.

The Journal of Cell Biology
|July 21, 2021
PubMed
Summary
This summary is machine-generated.

Researchers identified how the KIF1A motor protein selectively transports different vesicles in neurons. Specific motor domains, phosphorylation, and adaptors like MADD/Rab3GEP and Arl8A control cargo binding and neuronal transport.

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Related Experiment Videos

Last Updated: Oct 27, 2025

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Motors

Background:

  • Intracellular transport in neurons relies on molecular motors moving cargos along cytoskeletal tracks.
  • Understanding how these motors select specific cargo, such as dense core vesicles (DCVs), lysosomes, and synaptic vesicles (SVs), remains a challenge.

Purpose of the Study:

  • To investigate the selectivity and regulation of kinesin-3 family member KIF1A-driven transport.
  • To dissect the roles of KIF1A domains in motor activity and cargo binding.
  • To identify the adaptors responsible for linking KIF1A to specific vesicle types.

Main Methods:

  • Utilized engineered motors and cargo adaptors to study KIF1A transport.
  • Systematically analyzed KIF1A domain functions (CC1, CC2, CC3, PH).
  • Investigated the role of KIF1A phosphorylation in vesicle binding.
  • Identified specific adaptors (MADD/Rab3GEP, Arl8A) for different cargos.

Main Results:

  • KIF1A domains regulate autoinhibition (CC1), dimerization (CC2), and cargo binding (CC3, PH).
  • KIF1A phosphorylation is crucial for vesicle interaction.
  • MADD/Rab3GEP links KIF1A to SVs.
  • Arl8A mediates KIF1A interaction with DCVs and lysosomes.

Conclusions:

  • KIF1A cargo specificity is determined by distinct adaptors.
  • Motor dimerization, posttranslational modifications (phosphorylation), and specific adaptors regulate selective KIF1A cargo trafficking.
  • A model for regulated KIF1A-mediated transport of neuronal vesicles is proposed.