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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

BAI1-associated protein 2

IRSp53, insulin receptor substrate p53
The protein encoded by this gene has been identified as a brain-specific angiogenesis inhibitor (BAI1)-binding protein. This adaptor protein links membrane bound G-proteins to cytoplasmic effector proteins. This protein functions as an insulin receptor tyrosine kinase substrate and suggests a role for insulin in the central nervous system. It also associates with a downstream effector of Rho small G proteins, which is associated with the formation of stress fibers and cytokinesis. This protein is involved in lamellipodia and filopodia formation in motile cells and may affect neuronal growth-cone guidance. This protein has also been identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is associated with an autosomal dominant neurodegenerative disease. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: Actin, Insulin, Cdc42, Akt, Wasp
Papers on IRSp53
IRSp53/BAIAP2 in dendritic spine development, NMDA receptor regulation, and psychiatric disorders.
Review
New
Kim et al., Taejŏn, South Korea. In Neuropharmacology, Jan 2016
IRSp53 (also known as BAIAP2) is a multi-domain scaffolding and adaptor protein that has been implicated in the regulation of membrane and actin dynamics at subcellular structures, including filopodia and lamellipodia.
Yeast Ivy1p is a putative I-BAR-domain protein with pH-sensitive filament forming ability in vitro.
New
Suetsugu et al., Tokyo, Japan. In Cell Struct Funct, Jan 2016
The BAR domains with a convex surface form a subtype called the inverse BAR (I-BAR) domain or IRSp53-MIM-homology domain (IMD).
Severe learning deficits of IRSp53 mutant mice are caused by altered NMDA receptor dependent signal transduction.
New
Kreienkamp et al., Hamburg, Germany. In J Neurochem, Dec 2015
The insulin receptor substrate protein of 53 kDa (IRSp53, also known as Baiap2) is a signaling and adapter protein in forebrain excitatory synapses.
The flatness of Lamellipodia explained by the interaction between actin dynamics and membrane deformation.
New
Winkler et al., Vienna, Austria. In J Theor Biol, Oct 2015
This is motivated by observations of co-localization of proteins with I-BAR domains (like IRSp53) with polymerization and branching agents along the membrane.
Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells.
New
Muriaux et al., Lyon, France. In J Virol, Aug 2015
Our results revealed the involvement of activated Rac1 and of the IRSp53-Wave2-Arp2/3 signaling pathway in HIV-1 Gag membrane localization and particle release in T cells as well as a role for actin branching and polymerization, and this was solely dependent on the Gag viral protein.
Regulation of membrane-shape transitions induced by I-BAR domains.
New
Baumgart et al., Philadelphia, United States. In Biophys J, Aug 2015
I-BAR proteins contain an all-helical, crescent-shaped IRSp53-MIM domain (IMD) dimer that is believed to be able to couple with a membrane shape.
SH2B1 orchestrates signaling events to filopodium formation during neurite outgrowth.
New
Chen et al., Huazhou, China. In Commun Integr Biol, Jul 2015
Our recent findings suggest that SH2B1 can be recruited to the plasma membrane and F-actin fractions by IRSp53.
Social deficits in IRSp53 mutant mice improved by NMDAR and mGluR5 suppression.
New
Kim et al., Taejŏn, South Korea. In Nat Neurosci, Mar 2015
We found that mice lacking the excitatory synaptic signaling scaffold IRSp53 (also known as BAIAP2) showed impaired social interaction and communication.
IRSp53 senses negative membrane curvature and phase separates along membrane tubules.
Bassereau et al., Paris, France. In Nat Commun, 2014
The inverted-BAR (I-BAR) protein IRSp53, for instance, is found on the inner leaflet of the tubular membrane of filopodia; however its role in the formation of these structures is incompletely understood.
Insulin receptor substrate protein 53kDa (IRSp53) is a negative regulator of myogenic differentiation.
GeneRIF
Thanabalu et al., Singapore, Singapore. In Int J Biochem Cell Biol, 2012
propose that IRSp53 is a negative regulator of myogenic differentiation which correlates with the observed down regulation of IRSp53 expression during myoblast differentiation to myotubes
mDia1 and WAVE2 proteins interact directly with IRSp53 in filopodia and are involved in filopodium formation.
GeneRIF
Ahmed et al., Singapore, Singapore. In J Biol Chem, 2012
mDia1 and WAVE2 are important Src homology 3 domain partners of IRSp53 in forming filopodia.
Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.
GeneRIF
Stradal et al., Braunschweig, Germany. In Structure, 2011
Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli
The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
GeneRIF
Ciliberto et al., Milano, Italy. In Plos Comput Biol, 2011
Studied generation of filopodia with regards to the dynamic interaction established by Eps8, IRSp53 and VASP with actin filaments.
[A molecular dynamics study of the interaction between domain I-BAR of the IRSp53 protein and negatively charged membranes].
GeneRIF
Shaĭtan et al., In Biofizika, 2011
A molecular dynamics study of the interaction between domain I-BAR of the IRSp53 protein and negatively charged membranes
Subcellular membrane curvature mediated by the BAR domain superfamily proteins.
Review
Senju et al., Tokyo, Japan. In Semin Cell Dev Biol, 2010
The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily consists of proteins containing the BAR domain, the extended FCH (EFC)/FCH-BAR (F-BAR) domain, or the IRSp53-MIM homology domain (IMD)/inverse BAR (I-BAR) domain.
I-BAR domains, IRSp53 and filopodium formation.
Review
Bu et al., Singapore, Singapore. In Semin Cell Dev Biol, 2010
Cdc42 and its effector IRSp53 (insulin receptor phosphotyrosine 53 kDa substrate) have been shown to be strong inducers of filopodium formation.
IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions.
Review
Suetsugu et al., Milano, Italy. In Trends Cell Biol, 2008
A prototypical example of this type of proteins is the insulin receptor tyrosine kinase substrate of 53kDa, the founding member of a recently discovered family of proteins, including missing-in-metastasis and ABBA (actin-bundling protein with BAIAP2 homology).
The beta-thymosin/WH2 fold: multifunctionality and structure.
Review
Dominguez, Philadelphia, United States. In Ann N Y Acad Sci, 2007
This paper discusses the relationship between structure and function of the beta-thymosin/WH2 fold on the basis of four examples: (1) actin monomer sequestration (thymosin-beta4), (2) actin filament nucleation (WASP-Arp2/3 complex, Lmod, and spire), (3) actin filament elongation (Ena/VASP), and (4) cytoskeleton scaffolding (IRSp53 and MIM).
Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex.
Impact
GeneRIF
Scita et al., Milano, Italy. In Nat Cell Biol, 2006
These results support a model whereby the synergic bundling activity of the IRSp53-Eps8 complex, regulated by Cdc42, contributes to the generation of actin bundles, thus promoting filopodial protrusions.
IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling.
Impact
Takenawa et al., Tokyo, Japan. In Nature, 2001
Here we demonstrate that IRSp53, a substrate for insulin receptor with unknown function, is the 'missing link' between Rac and WAVE.
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