STRUCTURAL BASIS OF CELL MEMBRANE TARGETING, ADHESION, AND SIGNALING

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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. This program aims to determine the structures of proteins involved in cell membrane targeting, adhesion, and signaling, in order to establish the mechanism and specificity of their interactions. There are currently four projects with crystals that require synchrotron radiation. 1. Structure of full-length alpha-catenin, an F-actin binding protein that couples cadherin-based cell adhesion to regulation of the actin cytoskeleton. 2. The N-terminal domain of desmoplakin, a large protein that links desmosomal cadherins to intermediate filaments. 3. The Rab11 GTPase effector FIP3, involved in regulating targeting of recycling endosomal transport vesicles to the apical plasma membrane. 4. p97, a AAA+ ATPase responsible for removing misfolded proteins from the endoplasmic reticulum membrane, which also serves a model for the ATPase NSF responsible for disassembling SNARE complexes after membrane fusion.