Article
- The EMBO Journal (2006) 25, 693 - 700
- doi:10.1038/sj.emboj.7600965
Published online: 26 January 2006
Subject Categories:
Structural basis for myosin V discrimination between distinct cargoes
Natasha Pashkova1, Yui Jin1,2, S Ramaswamy1 and Lois S Weisman1,2
- Department of Biochemistry, University of Iowa, Iowa City, IA, USA
- Department of Cell and Developmental Biology and Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA
Correspondence to:
S Ramaswamy, Department of Biochemistry, The University of Iowa, Iowa City, IA 52242, USA. Tel.: +1 319 335 7917; Fax: +1 319 384 4770; E-mail: s-ramaswamy@uiowa.edu
Lois S Weisman, Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Room 6437, Ann Arbor, MI 48109-2216, USA. Tel.: +1 734 647 2539; Fax: +1 734 615 5493; E-mail: lweisman@umich.edu
Received 16 September 2005; Accepted 22 December 2005
Abstract
Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 Å of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180°. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors.
Keywords:
- cargo-binding domain,
- membrane transport,
- myosin V,
- Myo2p
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated
REVIEWS
PI3Kγ inhibition: towards an 'aspirin of the 21st century'?
Nature Reviews Drug Discovery Review (01 Nov 2006)
Oestrogen as a neuroprotective hormone
Nature Reviews Neuroscience Review (01 Jun 2002)
Organelles on the move: insights from yeast vacuole inheritance
Nature Reviews Molecular Cell Biology Review (01 Apr 2006)
RESEARCH
Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of mitochondria in the budding yeast
The EMBO Journal Article (07 Jul 2004)
Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
Nature Letters to Editor (06 Mar 2003)
