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Related Concept Videos

The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
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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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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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Related Experiment Video

Updated: May 13, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
08:06

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Structural basis for kinesin-1:cargo recognition.

Stefano Pernigo1, Anneri Lamprecht, Roberto A Steiner

  • 1Randall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK.

Science (New York, N.Y.)
|March 23, 2013
PubMed
Summary
This summary is machine-generated.

Researchers revealed how kinesin-1 motor proteins recognize and bind to specific cargo, like SKIP, using structural and biophysical methods. This discovery clarifies intracellular transport mechanisms crucial for cell function and disease.

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Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

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Related Experiment Videos

Last Updated: May 13, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
08:06

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Cargo Loading onto Kinesin Powered Molecular Shuttles
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Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
11:09

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

Published on: October 30, 2014

Area of Science:

  • Molecular biology
  • Cellular transport
  • Structural biology

Background:

  • Kinesin motor proteins are essential for intracellular cargo transport, a process vital for cellular functions and implicated in various diseases.
  • Understanding the molecular mechanisms of kinesin-cargo recognition is crucial for deciphering fundamental cellular processes and pathological pathways.

Purpose of the Study:

  • To determine the structural basis of kinesin light chain 2's interaction with cargo peptides containing the tryptophan-acidic motif.
  • To elucidate the molecular mechanisms underlying kinesin-1:cargo recognition.

Main Methods:

  • X-ray crystallography to obtain the structure of the kinesin light chain 2 tetratricopeptide repeat domain in complex with a cargo peptide.
  • Biophysical, biochemical, and cellular assays to validate the binding interactions and functional implications.

Main Results:

  • The crystal structure reveals the complex of kinesin light chain 2 with a tryptophan-acidic motif peptide derived from SKIP.
  • Structural and biophysical data support a model where kinesin-1 binds W-acidic cargo motifs via electrostatic interactions and sequence-specific elements.

Conclusions:

  • A framework for intracellular transport is proposed, based on kinesin-1's recognition of W-acidic cargo motifs.
  • Direct molecular evidence for kinesin-1:cargo recognition mechanisms has been provided, advancing the understanding of this fundamental cellular process.