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The activity of aminoacyl‐tRNA synthetase‐interacting multi‐functional protein 1 (AIMP1) on endothelial cells is mediated by the assembly of a cytoskeletal protein complex
Author(s) -
Jackson Valentina Charlotte,
Dewilde Sarah,
Albo Alessandra Giuliano,
Lis Katarzyna,
Corpillo Davide,
Canepa Barbara
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.23104
Subject(s) - microbiology and biotechnology , filamin , cytoskeleton , angiogenesis , immunoprecipitation , cell adhesion , biology , cell , chemistry , cell culture , biochemistry , cancer research , genetics
AIMP1 was first found as a factor associated with the aminoacyl‐tRNA synthetase (ARS) complex. However, it is also secreted and acts on different target cells such as endothelial cells, macrophages, and fibroblasts as an extracellular regulator, respectively, of angiogenesis, inflammatory responses and dermal regeneration. AIMP1 has also been reported to suppress in vivo tumor growth. In this study, we investigated the signaling pathways activated by exogenous AIMP1 in an in vitro endothelial model. AIMP1 decreases EC viability through an α5β1 integrin‐dependent mechanism and inhibits cell adhesion, is internalized and shows an asymmetric pattern of distribution and accumulation in cell protrusions. Experiments of affinity purification, pull down, and co‐immunoprecipitation showed that AIMP1 interacts with four cytoskeletal proteins (filamin‐A, α‐tubulin, vinculin, and cingulin). α‐Tubulin also gets phosphorylated upon cell treatment with AIMP1 and colocalization between AIMP1 and filamin‐A as well as between AIMP1 and cingulin was observed through immunofluorescence assays. In this work, we propose that AIMP1 effect on EC adhesion is mediated by the assembly of a cytoskeletal protein complex on the cytosolic face of the cell membrane which could regulate cellular architecture maintenance and remodeling. Moreover, this activity is able to indirectly influence cell viability. J. Cell. Biochem. 112: 1857–1868, 2011. © 2011 Wiley‐Liss, Inc.