Abstract：
:During yeast cell division, aggregates of damaged proteins are segregated asymmetrically between the bud and the mother. It is thought that protein aggregates are cleared from the bud via actin cable-based retrograde transport toward the mother and that Bni1p formin regulates this transport. Here, we examined the dynamics of Hsp104-associated protein aggregates by video microscopy, particle tracking, and image correlation analysis. We show that protein aggregates undergo random walk without directional bias. Clearance of heat-induced aggregates from the bud does not depend on formin proteins but occurs mostly through dissolution via Hsp104p chaperon. Aggregates formed naturally in aged cells also exhibit random walk but do not dissolve during observation. Although our data do not disagree with a role for actin or cell polarity in aggregate segregation, modeling suggests that their asymmetric inheritance can be a predictable outcome of aggregates' slow diffusion and the geometry of yeast cells.
journal_name
Celljournal_title
Cellauthors
Zhou C,Slaughter BD,Unruh JR,Eldakak A,Rubinstein B,Li Rdoi
10.1016/j.cell.2011.11.002subject
Has Abstractpub_date
2011-11-23 00:00:00pages
1186-96issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(11)01291-8journal_volume
147pub_type
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