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Published 31 January 2005. doi:10.1083/jcb.200407146
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 3, 359-364
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 Myosin V attachment to cargo requires the tight association of two functional subdomains

Natasha Pashkova1, Natalie L. Catlett1, Jennifer L. Novak1, Guanming Wu2, Renne Lu2, Robert E. Cohen1, and Lois S. Weisman1

1 Department of Biochemistry, University of Iowa, Iowa City, IA 52242
2 Boston Biomedical Research Institute, Watertown, MA 02472

Correspondence to Lois S. Weisman: lois-weisman{at}uiowa.edu


Abstract
The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle–specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V.

N.L. Catlett's present address is 737 Snapdragon St., Encinitas, CA 92024.

Abbreviations used in this paper: GAL4 AD, Gal4 DNA activation domain; GAL4 BD, Gal4 DNA-binding domain; MALDI-TOF, matrix-assisted laser desorption/ionization time of flight.


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