Abstract
Myosin VI is a reverse direction actin-based motor capable of taking large steps (30-36 nm) when dimerized. However, all dimeric myosin VI molecules so far examined have included nonnative coiled-coil sequences, and reports on full-length myosin VI have failed to demonstrate the existence of dimers. Herein, we demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 μm in ∼30 nm, hand-over-hand steps. Furthermore, we present data consistent with the monomers being prevented from dimerizing unless they are held in close proximity and that dimerization is somewhat inhibited by the cargo binding tail. A model thus emerges that cargo binding likely clusters and initiates dimerization of full-length myosin VI molecules. Although this mechanism has not been previously described for members of the myosin superfamily, it is somewhat analogous to the proposed mechanism of dimerization for the kinesin Unc104.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 331-336 |
| Number of pages | 6 |
| Journal | Molecular cell |
| Volume | 21 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 3 2006 |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering. / Park, Hyokeun; Ramamurthy, Bhagavathi; Travaglia, Mirko; Safer, Dan; Chen, Li Qiong; Franzini-Armstrong, Clara; Selvin, Paul R.; Sweeney, H. Lee.
In: Molecular cell, Vol. 21, No. 3, 03.02.2006, p. 331-336.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering
AU - Park, Hyokeun
AU - Ramamurthy, Bhagavathi
AU - Travaglia, Mirko
AU - Safer, Dan
AU - Chen, Li Qiong
AU - Franzini-Armstrong, Clara
AU - Selvin, Paul R.
AU - Sweeney, H. Lee
PY - 2006/2/3
Y1 - 2006/2/3
N2 - Myosin VI is a reverse direction actin-based motor capable of taking large steps (30-36 nm) when dimerized. However, all dimeric myosin VI molecules so far examined have included nonnative coiled-coil sequences, and reports on full-length myosin VI have failed to demonstrate the existence of dimers. Herein, we demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 μm in ∼30 nm, hand-over-hand steps. Furthermore, we present data consistent with the monomers being prevented from dimerizing unless they are held in close proximity and that dimerization is somewhat inhibited by the cargo binding tail. A model thus emerges that cargo binding likely clusters and initiates dimerization of full-length myosin VI molecules. Although this mechanism has not been previously described for members of the myosin superfamily, it is somewhat analogous to the proposed mechanism of dimerization for the kinesin Unc104.
AB - Myosin VI is a reverse direction actin-based motor capable of taking large steps (30-36 nm) when dimerized. However, all dimeric myosin VI molecules so far examined have included nonnative coiled-coil sequences, and reports on full-length myosin VI have failed to demonstrate the existence of dimers. Herein, we demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 μm in ∼30 nm, hand-over-hand steps. Furthermore, we present data consistent with the monomers being prevented from dimerizing unless they are held in close proximity and that dimerization is somewhat inhibited by the cargo binding tail. A model thus emerges that cargo binding likely clusters and initiates dimerization of full-length myosin VI molecules. Although this mechanism has not been previously described for members of the myosin superfamily, it is somewhat analogous to the proposed mechanism of dimerization for the kinesin Unc104.
UR - http://www.scopus.com/inward/record.url?scp=31544450256&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=31544450256&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2005.12.015
DO - 10.1016/j.molcel.2005.12.015
M3 - Article
C2 - 16455488
AN - SCOPUS:31544450256
VL - 21
SP - 331
EP - 336
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 3
ER -