Journal
BIOPHYSICAL JOURNAL
Volume 89, Issue 5, Pages 3589-3602Publisher
CELL PRESS
DOI: 10.1529/biophysj.105.065383
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Funding
- NCI NIH HHS [R56 CA101135, CA 101135, R01 CA101135] Funding Source: Medline
- NIGMS NIH HHS [GM 075305, R01 GM075305] Funding Source: Medline
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Lamellipodium extension, incorporating actin filament dynamics and the cell membrane, is simulated in three dimensions. The actin. lament network topology and the role of actin-associated proteins such as Arp2/3 are examined. We find that the orientational pattern of the. laments is in accord with the experimental data only if the spatial orientation of the Arp2/3 complex is restricted during each branching event. We hypothesize that branching occurs when Arp2/3 is bound to Wiskott-Aldrich syndrome protein (WASP), which is in turn bound to Cdc42 signaling complex; Arp2/3 binding geometry is restricted by the membrane-bound complex. Using mechanical and energetic arguments, we show that any membrane protein that is conical or trapezoidal in shape preferentially resides at the curved regions of the plasma membrane. We hypothesize that the transmembrane receptors involved in the recruitment of Cdc42/WASP complex has this property and concentrate at the leading edge. These features, combined with the mechanical properties of the cell membrane, explain why lamellipodium is a. at organelle.
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