Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins

Author:

MACHESKY M. Laura12,REEVES Emer1,WIENTJES Frans1,MATTHEYSE J. Frederick1,GROGAN Ann1,TOTTY F. Nicholas3,BURLINGAME L. Alma34,HSUAN J. Justin35,SEGAL W. Anthony1

Affiliation:

1. Department of Medicine, University College London, 5 University Street, London, W1P 8BT, U.K.

2. MRC-LMCB, University College London, Gower Street, London, WC1E 6BT, U.K.

3. Ludwig Institute for Cancer Research, 91 Riding House Street, London, W1P 8BT, U.K.

4. Department of Pharmaceutical Chemistry, The Mass Spectrometry Facility and Liver Center, University of California, San Francisco, CA, U.S.A., and Department of Biochemistry and Molecular Biology

5. University College London, Gower Street, London, WC1E 6BT, U.K.

Abstract

Human neutrophils contain a complex of proteins similar to the actin-related protein 2/3 (Arp2/3) complex of Acanthamoeba. We have obtained peptide sequence information for each member of the putative seven-protein complex previously described for Acanthamoeba and human platelets. From the peptide sequences we have identified cDNA species encoding three novel proteins in this complex. We find that in addition to Arp2 and Arp3, this complex contains a relative of the human (Suppressor of Profilin) SOP2Hs protein and four previously unknown proteins. These proteins localize in the cytoplasm of fibroblasts that lack lamellipodia, but are enriched in lamellipodia on stimulation with serum or platelet-derived growth factor. We propose a conserved and dynamic role for this complex in the organization of the actin cytoskeleton.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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