Feeling the tension in every step

Access through your institution Buy or subscribe Kinesin is a dimer, with two catalytic motor domains that are connected through a stalk to the cargo-binding C-terminal tail. Each motor head

is joined to the stalk by a flexible 'neck linker' that interacts with the motor. The neck linker drives the characteristic hand-over-hand 'stepping' movement of the two

kinesin heads, a mechanism that ensures that both heads do not dissociate from the microtubules simultaneously. So how do the neck linkers coordinate processive movement? > 

...coordination between the motor domains is mediated by > intramolecular tension... This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through

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Read our FAQs * Contact customer support REFERENCES ORIGINAL RESEARCH PAPER * Yildiz, A. et al. Intramolecular strain coordinates kinesin stepping behavior along microtubules. _Cell_ 134,

1030–1041 (2008) Article  CAS  PubMed Central  Google Scholar  FURTHER READING * Cochran, J.C. & Kull, F.J. Kinesin motors: no strain, no gain. _Cell_ 134, 918–919 (2008) Article  CAS 

PubMed Central  Google Scholar  Download references Authors * Ekat Kritikou View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS

Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Kritikou, E. Feeling the tension in every step. _Nat Rev Mol Cell Biol_ 9, 827 (2008). https://doi.org/10.1038/nrm2532 Download

citation * Published: 09 October 2008 * Issue Date: November 2008 * DOI: https://doi.org/10.1038/nrm2532 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this

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