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Related Concept Videos

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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...
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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,...
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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
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How kinesin waits between steps.

Teppei Mori1, Ronald D Vale, Michio Tomishige

  • 1Department of Applied Physics, The University of Tokyo, Tokyo 113-8656, Japan.

Nature
|November 16, 2007
PubMed
Summary
This summary is machine-generated.

Kinesin-1 motor proteins move along microtubules using a hand-over-hand motion. New smFRET sensors reveal kinesin-1 primarily uses a two-head-bound state during movement, switching to a one-head-bound state when ATP is scarce.

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Area of Science:

  • Molecular Motor Proteins
  • Cellular Transport Mechanisms
  • Biophysics

Background:

  • Kinesin-1 is a dimeric motor protein essential for intracellular transport along microtubules.
  • Its processive motility relies on ATP hydrolysis and a hand-over-hand motion of its two heads.
  • The 'waiting conformation' of kinesin-1 between steps, specifically the number of bound heads, is debated.

Purpose of the Study:

  • To investigate the binding state of kinesin-1 heads during processive movement.
  • To differentiate between one-head-bound and two-head-bound states of kinesin-1 on microtubules.
  • To elucidate the role of ATP concentration in kinesin-1's stepping mechanism.

Main Methods:

  • Development of two distinct single-molecule Förster Resonance Energy Transfer (smFRET) sensors.
  • Utilizing smFRET to detect the structural states of the kinesin-1 dimer during microtubule translocation.
  • Measuring kinesin-1 behavior under varying ATP concentrations.

Main Results:

  • Kinesin-1 predominantly adopts a two-head-bound conformation when ATP is saturating.
  • At low ATP concentrations, kinesin-1 enters a one-head-bound waiting state.
  • Brief transitions to a two-head-bound intermediate occur during movement at limiting ATP levels.

Conclusions:

  • The ATPase cycle and ATP availability dictate the head-binding states of kinesin-1.
  • A model is proposed where ATPase cycle transitions position heads for hand-over-hand motion.
  • This clarifies the mechanism underlying kinesin-1's processive motility.