RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes

• 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.

Nyckelord

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

Publikations- och innehållstyp

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