TY - JOUR
T1 - Force generation by endocytic actin patches in budding yeast
AU - Carlsson, Anders E.
AU - Bayly, Philip V.
N1 - Funding Information:
This work was supported by the National Institutes of Health under Grant No. R01-GM086882, and by the National Science foundation under Grant NO. PHY-1066293. We gratefully acknowledge the hospitality of the Aspen Center for Physics, where some of these ideas were developed.
PY - 2014/4/15
Y1 - 2014/4/15
N2 - Membrane deformation during endocytosis in yeast is driven by local, templated assembly of a sequence of proteins including polymerized actin and curvature-generating coat proteins such as clathrin. Actin polymerization is required for successful endocytosis, but it is not known by what mechanisms actin polymerization generates the required pulling forces. To address this issue, we develop a simulation method in which the actin network at the protein patch is modeled as an active gel. The deformation of the gel is treated using a finite-element approach. We explore the effects and interplay of three different types of force driving invagination: 1), forces perpendicular to the membrane, generated by differences between actin polymerization rates at the edge of the patch and those at the center; 2), the inherent curvature of the coat-protein layer; and 3), forces parallel to the membrane that buckle the coat protein layer, generated by an actomyosin contractile ring. We find that with optimistic estimates for the stall stress of actin gel growth and the shear modulus of the actin gel, actin polymerization can generate almost enough force to overcome the turgor pressure. In combination with the other mechanisms, actin polymerization can the force over the critical value.
AB - Membrane deformation during endocytosis in yeast is driven by local, templated assembly of a sequence of proteins including polymerized actin and curvature-generating coat proteins such as clathrin. Actin polymerization is required for successful endocytosis, but it is not known by what mechanisms actin polymerization generates the required pulling forces. To address this issue, we develop a simulation method in which the actin network at the protein patch is modeled as an active gel. The deformation of the gel is treated using a finite-element approach. We explore the effects and interplay of three different types of force driving invagination: 1), forces perpendicular to the membrane, generated by differences between actin polymerization rates at the edge of the patch and those at the center; 2), the inherent curvature of the coat-protein layer; and 3), forces parallel to the membrane that buckle the coat protein layer, generated by an actomyosin contractile ring. We find that with optimistic estimates for the stall stress of actin gel growth and the shear modulus of the actin gel, actin polymerization can generate almost enough force to overcome the turgor pressure. In combination with the other mechanisms, actin polymerization can the force over the critical value.
UR - http://www.scopus.com/inward/record.url?scp=84898856598&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2014.02.035
DO - 10.1016/j.bpj.2014.02.035
M3 - Article
C2 - 24739159
AN - SCOPUS:84898856598
SN - 0006-3495
VL - 106
SP - 1596
EP - 1606
JO - Biophysical Journal
JF - Biophysical Journal
IS - 8
ER -