Precise positioning of myosin VI on endocytic vesicles in vivo.

Abstract:

:Myosin VI has been studied in both a monomeric and a dimeric form in vitro. Because the functional characteristics of the motor are dramatically different for these two forms, it is important to understand whether myosin VI heavy chains are brought together on endocytic vesicles. We have used fluorescence anisotropy measurements to detect fluorescence resonance energy transfer between identical fluorophores (homoFRET) resulting from myosin VI heavy chains being brought into close proximity. We observed that, when associated with clathrin-mediated endocytic vesicles, myosin VI heavy chains are precisely positioned to bring their tail domains in close proximity. Our data show that on endocytic vesicles, myosin VI heavy chains are brought together in an orientation that previous in vitro studies have shown causes dimerization of the motor. Our results are therefore consistent with vesicle-associated myosin VI existing as a processive dimer, capable of its known trafficking function.

journal_name

PLoS Biol

journal_title

PLoS biology

authors

Altman D,Goswami D,Hasson T,Spudich JA,Mayor S

doi

10.1371/journal.pbio.0050210

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

e210

issue

8

eissn

1544-9173

issn

1545-7885

pii

06-PLBI-RA-1686

journal_volume

5

pub_type

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