TY - JOUR
T1 - DGKζ is involved in LPS-activated phagocytosis through IQGAP1/Rac1 pathway
AU - Okada, Masashi
AU - Hozumi, Yasukazu
AU - Iwazaki, Kiyoshi
AU - Misaki, Kentaro
AU - Yanagida, Mitsuaki
AU - Araki, Yoshihiko
AU - Watanabe, Takashi
AU - Yagisawa, Hitoshi
AU - Topham, Matthew K.
AU - Kaibuchi, Kozo
AU - Goto, Kaoru
N1 - Funding Information:
This work was supported by Grants-in-Aid from The Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan (M.O., Y.H., K.G.).
PY - 2012/4/6
Y1 - 2012/4/6
N2 - Diacylglycerol kinase (DGK) plays an important role in phosphoinositide signaling cascade by regulating the intracellular level of diacylglycerol and phosphatidic acid. The DGK family is involved in various pathophysiological responses that are mediated through unique binding partners in different tissues and cells. In this study, we identified a small GTPase effector protein, IQGAP1, as a novel DGKζ-associated complex protein. A bacterial endotoxin, lipopolysaccharide (LPS), facilitated the complex formation in macrophages. Both proteins co-localized at the edge and phagocytic cup of the cell. Furthermore, RNA interference-mediated knockdown of DGKζ or IQGAP1 impaired LPS-induced Rac1 activation. Primary macrophages derived from DGKζ-/- mice attenuated LPS-induced phagocytosis of bacteria. These results suggest that DGKζ is involved in IQGAP1/Rac1-mediated phagocytosis upon LPS stimulation in macrophages.
AB - Diacylglycerol kinase (DGK) plays an important role in phosphoinositide signaling cascade by regulating the intracellular level of diacylglycerol and phosphatidic acid. The DGK family is involved in various pathophysiological responses that are mediated through unique binding partners in different tissues and cells. In this study, we identified a small GTPase effector protein, IQGAP1, as a novel DGKζ-associated complex protein. A bacterial endotoxin, lipopolysaccharide (LPS), facilitated the complex formation in macrophages. Both proteins co-localized at the edge and phagocytic cup of the cell. Furthermore, RNA interference-mediated knockdown of DGKζ or IQGAP1 impaired LPS-induced Rac1 activation. Primary macrophages derived from DGKζ-/- mice attenuated LPS-induced phagocytosis of bacteria. These results suggest that DGKζ is involved in IQGAP1/Rac1-mediated phagocytosis upon LPS stimulation in macrophages.
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U2 - 10.1016/j.bbrc.2012.03.057
DO - 10.1016/j.bbrc.2012.03.057
M3 - Article
C2 - 22450320
AN - SCOPUS:84862817947
SN - 0006-291X
VL - 420
SP - 479
EP - 484
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -