Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16‐ARC/ARPC5
- 25 November 2002
- journal article
- research article
- Published by Wiley in Cell Motility
- Vol. 54 (1) , 81-90
- https://doi.org/10.1002/cm.10087
Abstract
The Arp2/3 complex is an actin filament nucleator that activates regulated actin assembly in response to extracellular signals. The mammalian complex is composed of seven subunits, the smallest of which is known as ARPC5 or p16‐Arc. We have identified a human cDNA sequence with homology to ARPC5 and here provide evidence that this encodes a novel ARPC5 isoform. Specific antibodies were generated against the novel protein, which we have termed ARPC5B, as well as the previously characterised ARPC5 isoform, henceforth ARPC5A. The presence of both ARPC5 isoforms was detected in Arp2/3 complex affinity purified from human neutrophil extract. The tissue distribution of ARPC5A and B was analysed using the isoform‐specific antibodies and it was found that the two isoforms exhibited significant differences; ARPC5A was found to be highly enriched in spleen and thymus, while ARPC5B exhibits a more regular expression, with levels in the brain being highest. Myc‐tagged ARPC5A and B co‐localised with the Arp2/3 complex when expressed in C2C12 cells and the cellular distribution of the two isoforms could not be distinguished. Our data show for the first time that mammalian cells contain multiple forms of the Arp2/3 complex. Cell Motil. Cytoskeleton 54:81–90, 2003.Keywords
Funding Information
- Medical Research Council and Cancer Research, UK
This publication has 25 references indexed in Scilit:
- A subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complexThe Journal of cell biology, 2002
- Crystal Structure of Arp2/3 ComplexScience, 2001
- Identification of Another Actin-related Protein (Arp) 2/3 Complex Binding Site in Neural Wiskott-Aldrich Syndrome Protein (N-WASP) That Complements Actin Polymerization Induced by the Arp2/3 Complex Activating (VCA) Domain of N-WASPJournal of Biological Chemistry, 2001
- Regulation of Actin Filament Network Formation Through ARP2/3 Complex: Activation by a Diverse Array of ProteinsAnnual Review of Biochemistry, 2001
- Activation of the Arp2/3 Complex by the Listeria ActA ProteinPublished by Elsevier ,2001
- Interactions among Subunits of Human Arp2/3 Complex: p20-Arc as the HubBiochemical and Biophysical Research Communications, 2001
- Integration of Multiple Signals Through Cooperative Regulation of the N-WASP-Arp2/3 ComplexScience, 2000
- Arp2/3 Complex and Actin Depolymerizing Factor/Cofilin in Dendritic Organization and Treadmilling of Actin Filament Array in LamellipodiaThe Journal of cell biology, 1999
- The Human Arp2/3 Complex Is Composed of Evolutionarily Conserved Subunits and Is Localized to Cellular Regions of Dynamic Actin Filament AssemblyThe Journal of cell biology, 1997
- Actin polymerization is induced by Arp 2/3 protein complex at the surface of Listeria monocytogenesNature, 1997