Myosin VI undergoes cargo-mediated dimerization.
Cell
; 138(3): 537-48, 2009 Aug 07.
Article
in En
| MEDLINE
| ID: mdl-19665975
ABSTRACT
Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Myosin Heavy Chains
Type of study:
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Cell
Year:
2009
Type:
Article
Affiliation country:
Hong Kong