RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes
2004 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 320, no 3, 1034-1042 p.Article in journal (Refereed) Published
RhoGAP interacting with CIP4 homologs-1 (RICH-1) was previously found in a yeast two-hybrid screen for proteins interacting with the SH3 domain of the Cdc42-interacting protein 4 (CIP4). RICH-1 was shown to be a RhoGAP for Cdc42 and Rac. In this study, we show that the BIN/Amphiphysin/Rvsp (BAR) domain in RICH-1 confers binding to membrane lipids, and has the potential to deform spherical liposomes into tubes. In accordance with previous findings for the BAR domains in endophilin and amphiphysin, RICH-1-induced tubes appeared striated. We propose that these striated structures are formed by oligomerization of RICH-1 through a putative coiled-coil region within the BAR domain. In support of this notion, we show that RICH-1 forms oligomers in the presence of the chemical cross-linker BS3. These results point to an involvement of RICH-1 in membrane deformation events.
Place, publisher, year, edition, pages
2004. Vol. 320, no 3, 1034-1042 p.
Amino Acid Sequence, Animals, Binding Sites, COS Cells, Cell Membrane/*metabolism/*ultrastructure, Cells; Cultured, Cercopithecus aethiops, Endothelial Cells/*metabolism, GTPase-Activating Proteins/*chemistry/*metabolism, Liposomes/*metabolism, Membrane Fluidity/*physiology, Membrane Lipids/*metabolism, Molecular Sequence Data, Nerve Tissue Proteins/chemistry/metabolism, Protein Binding, Protein Structure; Tertiary, Research Support; Non-U.S. Gov't, Research Support; U.S. Gov't; P.H.S., Sequence Homology; Amino Acid, Structure-Activity Relationship, Swine, Tissue Distribution
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-73074DOI: 10.1016/j.bbrc.2004.05.221PubMedID: 15240152OAI: oai:DiVA.org:uu-73074DiVA: diva2:100985