TY - JOUR
T1 - The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia
AU - Stradal, Theresia
AU - Courtney, Kevin D.
AU - Rottner, Klemens
AU - Hahne, Penelope
AU - Small, J. Victor
AU - Pendergast, Ann Marie
N1 - Funding Information:
This work was supported by a grant from the Austrian Science Foundation (to J.V.S.) and National Cancer Institute grant CA70940 (to A.M.P.). K.D.C. was supported by the Medical Scientist Training Program and the Department of Defense Breast Cancer Research Program. K.R. was supported by an EMBO fellowship. We thank Maria Schmittner for excellent technical assistance and Gunter Resch for help with electron microscopy. We thank David Sheeks for generating the web page. We thank Matthew Grove for technical advice. We thank Asier Echarri Aguirre and Alison Meloni for construct generation. We also thank Asier Echarri Aguirre for identification of the coiled-coil domain homology in Abi-1 and Abi-2b.
PY - 2001/6/5
Y1 - 2001/6/5
N2 - Cell movement is mediated by the protrusion of cytoplasm in the form of sheet- and rod-like extensions, termed lamellipodia and filopodia. Protrusion is driven by actin polymerization, a process that is regulated by signaling complexes that are, as yet, poorly defined. Since actin assembly is controlled at the tips of lamellipodia and filopodia [1], these juxtamembrane sites are likely to harbor the protein complexes that control actin polymerization dynamics underlying cell motility. An understanding of the regulation of protrusion therefore requires the characterization of the molecular components recruited to these sites. The Abl interactor (Abi) proteins, targets of Abl tyrosine kinases [2-4], have been implicated in Rac-dependent cytoskeletal reorganization in response to growth factor stimulation [5]. Here, we describe the unique localization of Abi proteins in living, motile cells. We show that Abi-1 and Abi-2b fused to enhanced yellow fluorescent protein (EYFP) are recruited to the tips of lamellipodia and filopodia. We identify the targeting domain as the homologous N terminus of these two proteins. Our findings are the first to suggest a direct involvement of members of the Abi protein family in the control of actin polymerization in protrusion events, and establish the Abi proteins as potential regulators of motility.
AB - Cell movement is mediated by the protrusion of cytoplasm in the form of sheet- and rod-like extensions, termed lamellipodia and filopodia. Protrusion is driven by actin polymerization, a process that is regulated by signaling complexes that are, as yet, poorly defined. Since actin assembly is controlled at the tips of lamellipodia and filopodia [1], these juxtamembrane sites are likely to harbor the protein complexes that control actin polymerization dynamics underlying cell motility. An understanding of the regulation of protrusion therefore requires the characterization of the molecular components recruited to these sites. The Abl interactor (Abi) proteins, targets of Abl tyrosine kinases [2-4], have been implicated in Rac-dependent cytoskeletal reorganization in response to growth factor stimulation [5]. Here, we describe the unique localization of Abi proteins in living, motile cells. We show that Abi-1 and Abi-2b fused to enhanced yellow fluorescent protein (EYFP) are recruited to the tips of lamellipodia and filopodia. We identify the targeting domain as the homologous N terminus of these two proteins. Our findings are the first to suggest a direct involvement of members of the Abi protein family in the control of actin polymerization in protrusion events, and establish the Abi proteins as potential regulators of motility.
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U2 - 10.1016/S0960-9822(01)00239-1
DO - 10.1016/S0960-9822(01)00239-1
M3 - Article
C2 - 11516653
AN - SCOPUS:0035811020
SN - 0960-9822
VL - 11
SP - 891
EP - 895
JO - Current Biology
JF - Current Biology
IS - 11
ER -