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Actin related protein 2/3 complex, subunit 4, 20kDa

ARPC4, p20-Arc, ARC20
This gene encodes one of seven subunits of the human Arp2/3 protein complex. This complex controls actin polymerization in cells and has been conserved throughout eukaryotic evolution. This gene encodes the p20 subunit, which is necessary for actin nucleation and high-affinity binding to F-actin. Alternative splicing results in multiple transcript variants. Naturally occurring read-through transcription exists between this gene and the downstream tubulin tyrosine ligase-like family, member 3 (TTLL3), which results in the production of a fusion protein. [provided by RefSeq, Nov 2010] (from NCBI)
Top mentioned proteins: Actin, Arp2, ARPC2, ARPC5, Actin-Related Protein 3
Papers on ARPC4
Comparative proteomic profiling of extracellular proteins between normal and gastric cancer cells.
Lim et al., Singapore, Singapore. In Curr Cancer Drug Targets, Jan 2016
Overexpression of ARPC4 was validated in gastric cell lines and its novel function in gastric cancer cell migration and invasion demonstrated in vitro.
Novel identification of Dermacentor variabilis Arp2/3 complex and its role in rickettsial infection of the arthropod vector.
Macaluso et al., Baton Rouge, United States. In Plos One, 2013
To investigate the role of the tick Arp2/3 complex in tick-Rickettsia interactions, open reading frames of all subunits of the protein including Arp2, Arp3, ARPC1, ARPC2, ARPC3, ARPC4, and ARPC5 were identified from Dermacentor variabilis.
Silencing of the ARP2/3 complex disturbs pancreatic cancer cell migration.
Kallioniemi et al., Tampere, Finland. In Anticancer Res, 2013
RESULTS: ARPC3 and ARPC4 were the most highly expressed complex members, while ARPC1B and ARPC2 were expressed at low levels.
Expression of the ARPC4 subunit of human Arp2/3 severely affects mycobacterium tuberculosis growth and suppresses immunogenic response in murine macrophages.
Ranganathan et al., New Delhi, India. In Plos One, 2012
METHODOLOGY/PRINCIPAL FINDINGS: Here we show that expression of ARPC4, a subunit of the Actin related protein 2/3 (Arp2/3) protein complex, severely affects the pathogen's growth.
Phosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activation.
Jacobson et al., San Francisco, United States. In Plos Comput Biol, 2011
The simulations suggest that phosphorylation causes reorientation of Arp2 relative to Arp3 by destabilizing a network of salt-bridge interactions at the interface of the Arp2, Arp3, and ARPC4 subunits.
Molecular dynamics simulations of Arp2/3 complex activation.
Pollard et al., New Haven, United States. In Biophys J, 2010
When we applied forces to Arp2 while restraining Arp3, one block of structure (Arp2, subunit ARPC1, the globular domain of ARPC4 and ARPC5) rotated counterclockwise by 30° around a pivot point in an α-helix of ARPC4 (Glu⁸¹-Asn¹⁰⁰) to align Arp2 next to Arp3 in a second block of structure including ARPC3 and the globular domains of ARPC2.
An actin-filament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability.
Welch et al., Berkeley, United States. In Proc Natl Acad Sci U S A, 2010
Using a combination of molecular dynamics and protein-protein docking simulations, we derived an independent structural model of the interaction between two subunits of the Arp2/3 complex that are key to actin binding, ARPC2 and ARPC4, and the side of an actin filament.
The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation.
Goode et al., Waltham, United States. In J Biol Chem, 2010
We identified three distinct sites on p40/ARPC1 required for function in vivo: one site contacts p19/ARPC4, one contacts p15/ARPC5, and one site resides in an extended structural "arm" of p40/ARPC1.
The association of the Arabidopsis actin-related protein2/3 complex with cell membranes is linked to its assembly status but not its activation.
Szymanski et al., West Lafayette, United States. In Plant Physiol, 2009
ARPC4 is the most critical core subunit that controls the assembly and steady-state levels of the complex.
Nucleotide- and activator-dependent structural and dynamic changes of arp2/3 complex monitored by hydrogen/deuterium exchange and mass spectrometry.
Almo et al., United States. In J Mol Biol, 2009
Changes in the rate of hydrogen exchange indicate that ATP binding causes conformational rearrangements of Arp2 and Arp3 that are transmitted allosterically to the Arp complex (ARPC)1, ARPC2, ARPC4, and ARPC5 subunits.
Functional surfaces on the p35/ARPC2 subunit of Arp2/3 complex required for cell growth, actin nucleation, and endocytosis.
Goode et al., Waltham, United States. In J Biol Chem, 2008
A second site required for nucleation and endocytosis was identified near the contact surface between p35/ARPC2 and p19/ARPC4.
BRICK1 is required for apical cell growth in filaments of the moss Physcomitrella patens but not for gametophore morphology.
Quatrano et al., Saint Louis, United States. In Plant Cell, 2008
Like BRK1, ARPC4 and At RABA4d are normally localized at the tip of apical cells and their localization is correlated with rapid tip growth in filaments.
Coronin 3 involvement in F-actin-dependent processes at the cell cortex.
Clemen et al., Köln, Germany. In Exp Cell Res, 2007
We show that coronin 3 similar to other coronins interacts with the Arp2/3-complex and cofilin indicating that this family in general is involved in regulating Arp2/3-mediated events.
The role of ARPC4 in tip growth and alignment of the polar axis in filaments of Physcomitrella patens.
Quatrano et al., Saint Louis, United States. In Cell Motil Cytoskeleton, 2006
When the actin related protein 2/3 (Arp2/3) complex member arpc4 was deleted in Physcomitrella patens (moss), the resulting null mutant (Deltaarpc4) was viable and revealed no gross changes during morphogenesis of filaments into gametophores.
Crystal structure of Arp2/3 complex.
Pollard et al., Los Angeles, United States. In Science, 2001
Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal alpha helices and have similarly folded amino-terminal alpha/beta domains.
Etanercept in the treatment of psoriatic arthritis and psoriasis: a randomised trial.
Burge et al., Seattle, United States. In Lancet, 2000
The ARC20 was achieved by 22 (73%) of etanercept-treated patients compared with four (13%) of placebo-treated patients.
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