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Title: Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI

Abstract

Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take {approx}36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single {alpha}-helix of {approx}10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the {approx}36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization.

Authors:
; ; ; ;  [1]
  1. Stanford
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006723
Resource Type:
Journal Article
Journal Name:
Nat. Struct. Mol. Biol.
Additional Journal Information:
Journal Volume: 15; Journal Issue: (6) ; 2008; Journal ID: ISSN 1545-9993
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ACTIN; CARGO; DIMERIZATION; HYPOTHESIS; MONOMERS; MYOSIN

Citation Formats

Spink, Benjamin J, Sivaramakrishnan, Sivaraj, Lipfert, Jan, Doniach, Sebastian, and Spudich, James A. Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI. United States: N. p., 2008. Web. doi:10.1038/nsmb.1429.
Spink, Benjamin J, Sivaramakrishnan, Sivaraj, Lipfert, Jan, Doniach, Sebastian, & Spudich, James A. Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI. United States. https://doi.org/10.1038/nsmb.1429
Spink, Benjamin J, Sivaramakrishnan, Sivaraj, Lipfert, Jan, Doniach, Sebastian, and Spudich, James A. 2008. "Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI". United States. https://doi.org/10.1038/nsmb.1429.
@article{osti_1006723,
title = {Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI},
author = {Spink, Benjamin J and Sivaramakrishnan, Sivaraj and Lipfert, Jan and Doniach, Sebastian and Spudich, James A},
abstractNote = {Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take {approx}36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single {alpha}-helix of {approx}10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the {approx}36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization.},
doi = {10.1038/nsmb.1429},
url = {https://www.osti.gov/biblio/1006723}, journal = {Nat. Struct. Mol. Biol.},
issn = {1545-9993},
number = (6) ; 2008,
volume = 15,
place = {United States},
year = {Mon Sep 29 00:00:00 EDT 2008},
month = {Mon Sep 29 00:00:00 EDT 2008}
}