ABM-1 and ABM-2 homology sequences: consensus docking sites for actin-based motility defined by oligoproline regions in Listeria ActA surface protein and human VASP.
Actin-based motility involves a cascade of binding interactions designed to assemble actin regulatory proteins into functional locomotory units. Listeria ActA surface protein contains a series of nearly identical EFPPPPTDE-type oligoproline sequences for binding vasodilator-stimulated phosphoprotein (VASP). The latter is a tetrameric protein with numerous GPP-PPP docking sites for profilin, a 15 kDa regulatory protein that promotes actin filament assembly. Analysis of known actin regulatory proteins led to the identification of distinct Actin-Based Motility homology sequences ABM-1; (D/E)FPPPPX(D/E); and ABM-2, XPPPPP (where X denotes G, A, L, and S).
Purich
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Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610-0245, USA.
Southwick
F S
FS
D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D016384:Consensus Sequence; D003285:Contractile Proteins; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D008840:Microfilament Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000737:chemistry*; D051304:Profilins; D011392:Proline / Q000737:chemistry; D011485:Protein Binding; D000098662:Vasodilator-Stimulated Phosphoprotein
D000199:Actins; D001426:Bacterial Proteins; D015815:Cell Adhesion Molecules; D003285:Contractile Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D010750:Phosphoproteins; D051304:Profilins; D000098662:Vasodilator-Stimulated Phosphoprotein; C072980:actA protein, Listeria monocytogenes; D011392:Proline