Structural and viscoelastic properties of actin networks formed by espin or pathologically relevant espin mutants.
The structural organization of the cytoskeleton determines its viscoelastic response which is crucial for the correct functionality of living cells. Both the mechanical response and microstructure of the cytoskeleton are regulated on a microscopic level by the local activation of different actin binding and/or bundling proteins (ABPs). Misregulations in the expression of these ABPs or mutations in their sequence can entail severe cellular dysfunctions and diseases. Here, we study the structural and viscoelastic properties of reconstituted actin networks cross-linked by the ABP espin and compare the obtained network properties to those of other bundled actin networks. Moreover, we quantify the impact of pathologically relevant espin mutations on the viscoelastic properties of these cytoskeletal networks.
Lieleg
Oliver
O
Faculty of Arts and Sciences, Center for Systems Biology, Harvard University, Cambridge, MA, USA.
Schmoller
Kurt M
KM
Purdy Drew
Kirstin R
KR
Claessens
Mireille M A E
MM
Semmrich
Christine
C
Zheng
Lili
L
Bartles
James R
JR
Bausch
Andreas R
AR
D000199:Actins / Q000737:chemistry*; D000818:Animals; D003599:Cytoskeleton; D004548:Elasticity; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry
D000199:Actins; C493274:ESPN protein, human; D008840:Microfilament Proteins; D011994:Recombinant Proteins