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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
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...
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,...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
The Mitotic Spindle02:27

The Mitotic Spindle

The mitotic spindle—or spindle apparatus—is a eukaryotic, cytoskeletal structure made up of long protein fibers called microtubules. Formed during cell division, the spindle separates sister chromatids and moves them to opposite ends of a parental cell, where the now individual chromosomes are distributed to two daughter cell nuclei.
The bipolar configuration of the mitotic spindle facilitates chromosomal segregation, preparing the cell for division. One mechanism that ensures bipolar mitotic...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...

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Articles linked to this work by shared authors, journal, and citation graph.

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Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.

The EMBO journal·2001
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Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa.

The EMBO journal·2001
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Walking on two heads: the many talents of kinesin.

Nature reviews. Molecular cell biology·2001
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Molecular motors. Switching on kinesin.

Nature·2001
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Surface topography of microtubule walls decorated with monomeric and dimeric kinesin constructs.

Biological chemistry·2000
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Cargo binding and regulatory sites in the tail of fungal conventional kinesin.

Nature cell biology·2000
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Related Experiment Video

Updated: Jul 15, 2026

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

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

A look into kinesin's powerhouse.

G Woehlke1

  • 1Institute for Cell Biology, Ludwig-Maximilians-University, Schillerstr. 42, D-80336, Munich, Germany. guenther.woehlke@irz.uni-muenchen.de

FEBS Letters
|December 1, 2001
PubMed
Summary

Kinesin motor proteins utilize switch regions for microtubule binding and energy conversion. Structural and mutational studies reveal how these regions modulate motor function and nucleotide state.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Kinesins are microtubule-dependent motor proteins essential for cellular functions.
  • Their conserved motor domain generates energy for movement.
  • Structural similarities to myosin and G-proteins suggested functional roles for specific regions.

Purpose of the Study:

  • To investigate the role of kinesin switch I and II regions in the catalytic mechanism.
  • To understand how these regions mediate communication between the nucleotide-binding site and microtubule interaction.
  • To explore the structural basis of microtubule affinity modulation.

Main Methods:

  • Analysis of high-resolution crystal structures of kinesin motor domains.
  • Mutational analyses of switch regions.

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Related Experiment Videos

Last Updated: Jul 15, 2026

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

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

  • Comparison of different nucleotide-bound states (ADP and ATP-like).
  • Main Results:

    • Switch regions (I and II) are crucial for kinesin's catalytic mechanism and motor function.
    • Variable conformations of switch regions were observed in different structural states.
    • A helix adjacent to switch II significantly influences microtubule binding affinity.
    • Mutations in switch regions correlate structural changes with altered microtubule binding and nucleotide state coupling.

    Conclusions:

    • Kinesin switch regions are critical for coupling nucleotide hydrolysis to mechanical work and microtubule binding.
    • Structural plasticity in these regions allows for dynamic regulation of motor activity.
    • Understanding switch region function provides insights into kinesin mechanism and potential therapeutic targets.