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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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,...
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

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Related Experiment Video

Updated: May 21, 2026

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
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Kinesin tail domains are intrinsically disordered.

Mark A Seeger1, Yongbo Zhang, Sarah E Rice

  • 1Department of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.

Proteins
|June 8, 2012
PubMed
Summary

Kinesin motor proteins utilize intrinsic disorder in their nonmotor regions, particularly tails, for specific cargo transport. This structural feature is common across all human kinesins and essential for their function.

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Published on: February 14, 2016

Area of Science:

  • Molecular biology
  • Biophysics
  • Structural biology

Background:

  • Kinesin motor proteins are essential for intracellular transport, utilizing motor domains for force generation along microtubules.
  • Nonmotor regions, especially tails, dictate cargo specificity and are modulated by cellular signals.
  • Sequence divergence in nonmotor regions suggests diverse functional roles.

Purpose of the Study:

  • To investigate the prevalence and functional significance of intrinsic disorder in human kinesin proteins.
  • To determine if intrinsically disordered regions are common across the kinesin superfamily.
  • To experimentally validate the role of intrinsic disorder in kinesin tail domains.

Main Methods:

  • Bioinformatic analysis of full-length human kinesin sequences to predict intrinsically disordered regions.
  • Expression and purification of tail domains from Kif5B, Kif10, and KifC3 kinesin families.
  • Circular dichroism (CD) and Nuclear Magnetic Resonance (NMR) spectroscopy to assess the structural properties of isolated tail domains.

Main Results:

  • Bioinformatic analysis predicted significant intrinsically disordered regions in all 43 human kinesins, concentrated in nonmotor domains like tails.
  • Experimental data confirmed that isolated kinesin tail domains are intrinsically disordered in vitro.
  • These disordered tail domains retained their ability to bind microtubules, indicating functional relevance.

Conclusions:

  • Intrinsic disorder is a common structural feature of human kinesins, particularly in their nonmotor regions.
  • This intrinsic disorder is crucial for conferring functional specificity to kinesins in cargo transport.
  • The findings provide a new perspective on the structural basis of kinesin diversity and function.