Format

Send to

Choose Destination
J Biol Chem. 2013 Nov 22;288(47):34131-45. doi: 10.1074/jbc.M113.507202. Epub 2013 Oct 4.

Structural insights into functional overlapping and differentiation among myosin V motors.

Author information

1
From the Brazilian Biosciences National Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo 13083-100, Brazil.

Abstract

Myosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes, and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb, and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned, indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high resolution insights into motor domain inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, autoinhibition, and regulatory mechanisms in myosin V motors.

KEYWORDS:

Cargo-binding Domain; Cell Signaling; Crystal Structure; Intracellular Trafficking; Molecular Motors; Molecular Plasticity; Myosin; Myosin V; Redox Dimerization

PMID:
24097982
PMCID:
PMC3837155
DOI:
10.1074/jbc.M113.507202
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center