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 Bioljournal_title
PLoS biologyauthors
Altman D,Goswami D,Hasson T,Spudich JA,Mayor Sdoi
10.1371/journal.pbio.0050210subject
Has Abstractpub_date
2007-08-01 00:00:00pages
e210issue
8eissn
1544-9173issn
1545-7885pii
06-PLBI-RA-1686journal_volume
5pub_type
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