Abstract
Understanding how specific proteins manipulate the shape and form of membranes is crucial to understanding key biological functions. Membrane curvature generation enables the creation of structures such as intracellular transport vesicles, and also guides geometry-dependent protein localization. We focus on Sar1, a roughly 21.5 kDa GTPase of the COPII family of coat proteins, which initiates the assembly of coated vesicles at the endoplasmic reticulum. Our recent work has shown that the yeast (S. cerevisiae) Sar1p dramatically lowers membrane rigidity, and has an energetic preference for concave curvature (Settles et. al. Biophysical Journal, 99(5) pp. 1539 - 1545). Exploring the structurally similar mammalian Sar1 paralogs Sar1a and Sar1b, using both optical-trap based assays involving dynamic membrane deformation and microfabricated surfaces that present controlled curvatures to the proteins, we quantify the mechanical properties of Sar1-membrane interactions and delineate differences in the abilities of these proteins to lower the membrane bending modulus.
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