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RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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
Abstract [en]

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.
Keyword [en]
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
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-73074DOI: 10.1016/j.bbrc.2004.05.221PubMedID: 15240152OAI: oai:DiVA.org:uu-73074DiVA: diva2:100985
Available from: 2005-05-31 Created: 2005-05-31 Last updated: 2013-11-07Bibliographically approved

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Fransson, ÅsaAspenström, Pontus

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