Actomyosin contractility is essential for biological force generation, and is
well understood in highly organized structures such as striated muscle.
Additionally, actomyosin bundles devoid of this organization are known to
contract both in vivo and in vitro, which cannot be described by standard
muscle models. To narrow down the search for possible contraction mechanisms in
these systems, we investigate their microscopic symmetries. We show that
contractile behavior requires non-identical motors that generate large enough
forces to probe the nonlinear elastic behavior of F-actin. This suggests a role
for filament buckling in the contraction of these bundles, consistent with
recent experimental results on reconstituted actomyosin bundles.Comment: 10 pages, 6 figures; text shortene