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Spatiotemporal mechanisms for actomyosin ring assembly and contraction in budding yeast cell division
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Animal and yeast cells use a contractile ring that is
attached to the plasma membrane to create a cleavage furrow
that partitions a cell into two in the latest step of cell division. The
contractile ring is a network of actin and myosin-II motor
filaments embedded in a complex and compact protein core
structure at the cell division site. In the absence of myosin-II,
cells fail to assemble the contractile ring pursuing death or rapidly
evolving divergent pathways to restore growth and cytokinesis,
an event associated to aneuploidy, a common trait in cancer
development and progression. The molecular mechanisms
underlying myosin-II localization and function at the cell division
site with actin ring assembly and contraction remain poorly
understood. Based on analogy to the striated muscle, it has been
classically proposed that contractile stress in the actomyosin ring
is generated via a “sliding filament” mechanism in which bipolar
myosin-II motor filaments walk along actin filaments, within
organized sarcomere-like arrays. However, ultra-structural and
genetic studies in different cellular systems have shown that
contractile rings are more complex than striated muscles, and in
some examples the motor activity can actually be dispensable for
the contractibility of the cytokinetic ring.(...)
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Dissertation presented to obtain the Ph.D degree in Molecular Medicine
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Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica