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

Richnau, Ninna; Fransson, Åsa; Farsad, Khashayar; Aspenström, Pontus

doi:10.1016/j.bbrc.2004.05.221

Cited by 48 publications

(41 citation statements)

References 24 publications

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“…Furthermore, several BAR-domain-containing RhoGAPs exist, such as RICH1, which has GAP activity for Cdc42 and Rac1. RICH1 binds the F-BAR-domain protein CIP4, which is structurally similar to the PACSIN proteins (Richnau et al, 2004;Richnau and Aspenstrom, 2001). We are currently pursuing this issue to determine the localization and relevance of selected Rac GAPs, although these studies are complicated by the number of GAPs (Bernards, 2003) and the limited availability of sufficient well-characterized reagents.…”

Section: Discussionmentioning

confidence: 99%

The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

Kreuk

Nethe

Fernandez‐Borja

et al. 2011

Journal of Cell Science

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The Rac1 GTPase controls cytoskeletal dynamics and is a key regulator of cell spreading and migration mediated by signaling through effector proteins, such as the PAK kinases and the Scar and WAVE proteins. We previously identified a series of regulatory proteins that associate with Rac1 through its hypervariable C-terminal domain, including the Rac1 activator β-Pix (also known as Rho guanine-nucleotide-exchange factor 7) and the membrane adapter caveolin-1. Here, we show that Rac1 associates, through its C-terminus, with the F-BAR domain protein PACSIN2, an inducer of membrane tubulation and a regulator of endocytosis. We show that Rac1 localizes with PACSIN2 at intracellular tubular structures and on early endosomes. Active Rac1 induces a loss of PACSIN2-positive tubular structures. By contrast, Rac1 inhibition results in an accumulation of PACSIN2-positive tubules. In addition, PACSIN2 appears to regulate Rac1 signaling; siRNA-mediated loss of PACSIN2 increases the levels of Rac1-GTP and promotes cell spreading and migration in a wound healing assay. Moreover, ectopic expression of PACSIN2 reduces Rac1-GTP levels in a fashion that is dependent on the PACSIN2–Rac1 interaction, on the membrane-tubulating capacity of PACSIN2 and on dynamin. These data identify the BAR-domain protein PACSIN2 as a Rac1 interactor that regulates Rac1-mediated cell spreading and migration.

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Section: Discussionmentioning

confidence: 99%

The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

Kreuk

Nethe

Fernandez‐Borja

et al. 2011

Journal of Cell Science

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“…RICH-1 is also known as nadrin 1. RICH-1 possesses an N-terminal amphipathic ␣-helix homologous to that in endophilin A1 and B1 that mediates high-affinity liposome binding and tubulation as well as a BAR domain and has been confirmed to have liposome-binding and tubulating activity in vitro (73,237,264). RICH-1 localizes to the ER: in contrast to amphiphysin 1 and Bin1 isoforms, RICH-1 does not localize to either the plasma membrane or endosomes.…”

Section: Rich-1/nadrinmentioning

confidence: 99%

“…RICH-1 localizes to the ER: in contrast to amphiphysin 1 and Bin1 isoforms, RICH-1 does not localize to either the plasma membrane or endosomes. An interesting feature of RICH-1 is the ability of its isolated BAR domain to directly bind phosphoinositides in vitro, including PtdIns, PtdIns(3)P, PtdIns(4)P, PtdIns(5)P, PtdIns(3,5)P2, and PtdIns(4,5)P2 as well as other phospholipids, including phosphatidylserine and phosphatidic acid on a solid support (264). The specificity of binding to these lipids has not yet been tested using more physiological assays such as liposome binding, and it is possible that the BAR domain is recognizing predominantly negative charge rather than these specific lipids.…”

Section: Rich-1/nadrinmentioning

confidence: 99%

“…We now know that BAR domains bind and tubulate membranes both in vitro and also in vivo (73,264,316,380). Furthermore, crystallography has revealed that BAR domains are banana-shaped dimers able to sense and (depending on the presence of other membrane-binding domains) create membrane curvature (237).…”

Section: Membrane Tubulation and Bar Domain Protein Function In Vivomentioning

confidence: 99%

“…For example, RICH-1 has been shown to localize to the ER and to play a role in tubule formation at this organelle (73,264). Endophilin B1 tubulates Golgi apparatus membranes (73) while SNX1 plays a role in tubule formation at the early endosome (25).…”

Section: Membrane Tubulation and Bar Domain Protein Function In Vivomentioning

confidence: 99%

See 2 more Smart Citations

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Ren

Vajjhala

Lee

et al. 2006

Microbiol Mol Biol Rev

194

186

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SUMMARY The Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.

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dAsap regulates cellular protrusions via an Arf6‐dependent actin regulatory pathway in S2R+ cells

Kushwaha,

Mallik,

Bisht

et al. 2024

FEBS Letters

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Membrane protrusions are fundamental to cellular functions like migration, adhesion, and communication and depend upon dynamic reorganization of the cytoskeleton. GAP‐dependent GTP hydrolysis of Arf proteins regulates actin‐dependent membrane remodeling. Here, we show that dAsap regulates membrane protrusions in S2R+ cells by a mechanism that critically relies on its ArfGAP domain and relocalization of actin regulators, SCAR, and Ena. While our data reinforce the preference of dAsap for Arf1 GTP hydrolysis in vitro, we demonstrate that induction of membrane protrusions in S2R+ cells depends on Arf6 inactivation. This study furthers our understanding of how dAsap‐dependent GTP hydrolysis maintains a balance between active and inactive states of Arf6 to regulate cell shape.

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

Cited by 48 publications

References 24 publications

The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

dAsap regulates cellular protrusions via an Arf6‐dependent actin regulatory pathway in S2R+ cells

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