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Interaction and localization of Necl‐5 and PDGF receptor β at the leading edges of moving NIH3T3 cells: Implications for directional cell movement
Author(s) -
Amano Hisayuki,
Ikeda Wataru,
Kawano Satoshi,
Kajita Mihoko,
Tamaru Yoshiyuki,
Inoue Naoya,
Minami Yukiko,
Yamada Akio,
Takai Yoshimi
Publication year - 2008
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2008.01167.x
Subject(s) - integrin , platelet derived growth factor receptor , microbiology and biotechnology , biology , lamellipodium , receptor , vitronectin , focal adhesion , cell migration , signal transduction , cell , growth factor , biochemistry
It was previously shown that platelet‐derived growth factor (PDGF) receptor physically and functionally interacts with integrin α v β 3 , effectively inducing cell movement. We previously showed that Necl‐5, originally identified as a poliovirus receptor, interacts with integrin α v β 3 and enhances its clustering and the formation of focal complexes at the leading edges of moving cells, resulting in an enhancement of cell movement. We showed here that Necl‐5 additionally interacts with PDGF receptor in NIH3T3 cells and regulates the interaction between PDGF receptor and integrin α v β 3 , effectively inducing directional cell movement. PDGF receptor co‐localized with Necl‐5 and integrin α v β 3 at peripheral ruffles over lamellipodia, which were formed at the leading edges of moving cells in response to PDGF, but not at the focal complexes under these ruffles, whereas Necl‐5 and integrin α v β 3 co‐localized at these focal complexes. The clustering of these three molecules at peripheral ruffles required the activation of integrin α v β 3 by vitronectin and the PDGF‐induced activation of the small G protein Rac and subsequent re‐organization of the actin cytoskeleton. These results indicate a key role of Necl‐5 in directional cell movement by physically and functionally interacting with both integrin α v β 3 and PDGF receptor.