Abstract:
:The assembly of actin monomers into filaments and networks plays vital roles throughout eukaryotic biology, including intracellular transport, cell motility, cell division, determining cellular shape, and providing cells with mechanical strength. The regulation of actin assembly and modulation of filament mechanical properties are critical for proper actin function. It is well established that physiological salt concentrations promote actin assembly and alter the overall bending mechanics of assembled filaments and networks. However, the molecular origins of these salt-dependent effects, particularly if they involve nonspecific ionic strength effects or specific ion-binding interactions, are unknown. Here, we demonstrate that specific cation binding at two discrete sites situated between adjacent subunits along the long-pitch helix drive actin polymerization and determine the filament bending rigidity. We classify the two sites as "polymerization" and "stiffness" sites based on the effects that mutations at the sites have on salt-dependent filament assembly and bending mechanics, respectively. These results establish the existence and location of the cation-binding sites that confer salt dependence to the assembly and mechanics of actin filaments.
journal_name
Proc Natl Acad Sci U S Aauthors
Kang H,Bradley MJ,McCullough BR,Pierre A,Grintsevich EE,Reisler E,De La Cruz EMdoi
10.1073/pnas.1211078109subject
Has Abstractpub_date
2012-10-16 00:00:00pages
16923-7issue
42eissn
0027-8424issn
1091-6490pii
1211078109journal_volume
109pub_type
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