The myosin in question, Myo5, is a class I myosin from budding yeast. The Boston group found that Myo5 had unusual dynamics: it was stationary at cortical actin patches, the presumptive endocytic sites in yeast, and departed after only a brief stay. The peak of Myo5 localization came immediately before the actin polymerization factor Arp2 switched from slow to fast movement away from the membrane. This switch was delayed (although the fast phase, once started, was normal) when Myo5 was mutant.
Previous workers have defined a sequence of comings and goings of different components at the actin patches. Some of these components are thought to move away from the...
The Rockefeller University Press
2004
The Rockefeller University Press
2004
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