This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Proteins from the BAR domain superfamily [1], ubiquitous in many organisms and cell types (, are implicated in a multitude of cellular processes involving membrane remodeling, e.g., endocytosis, apoptosis, and cell-cell fusion. In vitro, these proteins sculpt high-curvature membrane tubes and vesicles [2, 3] from low- curvature liposomes. BAR domains form banana-shaped homodimers bearing a high density of positively charged residues on the concave surface [4?6], which facilitates sculpting of negatively charged membranes. However, single BAR domains induce only local membrane curvature [7, 8], while recent cryo-EM reconstructions [3] reveal that sculpting of membrane tubes and vesicles is performed by many BAR domains arranged in lattice-like scaffolds.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-E (40))
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University of Illinois Urbana-Champaign
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