Involvement of FAK/Src complex in the processes of <i>Escherichia coli</i> phagocytosis by insect hemocytes

Metheniti, Aristea; Paraskevopoulou, Nikolitsa; Lambropoulou, María; Marmaras, Vassilis J.

doi:10.1016/s0014-5793(01)02405-x

Cited by 37 publications

(37 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…On the other hand, the binding of Trol seemed to activate integrin and increase the level of FAK phosphorylation. The requirement of FAK has been shown for mammals in the integrin ␣ v ␤ 5 -mediated phagocytosis of apoptotic cells (43) or spent photoreceptor outer segment fragments (44) and for insects in the integrin-mediated phagocytosis of bacteria (45). Therefore, it is possible that phosphorylated FAK is included in a signaling pathway activated by integrin ␤, although INA-1 does not seem to need FAK to induce phagocytosis (17).…”

Section: Discussionmentioning

confidence: 99%

Integrin βν-mediated Phagocytosis of Apoptotic Cells in Drosophila Embryos

Nagaosa

Okada

Nonaka

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

To identify molecules that play roles in the clearance of apoptotic cells by Drosophila phagocytes, we examined a series of monoclonal antibodies raised against larval hemocytes for effects on phagocytosis in vitro. One antibody that inhibited phagocytosis recognized terribly reduced optic lobes (Trol), a core protein of the perlecan-type proteoglycan, and the level of phagocytosis in embryos of a Trol-lacking fly line was lower than in a control line. The treatment of a hemocyte cell line with a recombinant Trol protein containing the amino acid sequence RGD augmented the phosphorylation of focal adhesion kinase, a hallmark of integrin activation. A loss of integrin ␤, one of the two ␤ subunits of Drosophila integrin, brought about a reduction in the level of apoptotic cell clearance in embryos. The presence of integrin ␤ at the surface of embryonic hemocytes was confirmed, and forced expression of integrin ␤ in hemocytes of an integrin ␤-lacking fly line recovered the defective phenotype of phagocytosis. Finally, the level of phagocytosis in a fly line that lacks both integrin ␤ and Draper, another receptor required for the phagocytosis of apoptotic cells, was lower than that in a fly line lacking either protein. We suggest that integrin ␤ serves as a phagocytosis receptor responsible for the clearance of apoptotic cells in Drosophila, independent of Draper.

show abstract

Section: Discussionmentioning

confidence: 99%

Integrin βν-mediated Phagocytosis of Apoptotic Cells in Drosophila Embryos

Nagaosa

Okada

Nonaka

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In insect hemocytes, antibody-mediated inhibition of Src and FAK has been shown to abolish FAK phosphorylation and phagocytosis of E. coli (38). In retina, daily ␣v␤5 integrin-dependent phagocytosis of spent photoreceptor outer segment fragments by the retinal pigment epithelium was crucial for retinal function, and FAK was pivotal in this process (39).…”

Section: Discussionmentioning

confidence: 99%

Eps8 Protein Facilitates Phagocytosis by Increasing TLR4-MyD88 Protein Interaction in Lipopolysaccharide-stimulated Macrophages

Chen

Hsieh

Chang

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: TLR4-mediated p38 MAPK and actin cytoskeleton reorganization are important for macrophage phagocytosis. Results: TLR4-induced Eps8 facilitates TLR4-MyD88 interaction, leading to the activation of p38 MAPK, actin polymerization, and the uptake of bacteria in macrophages. Conclusion: Eps8 is critical in innate immunity. Significance: This is the first report to indicate that Eps8 contributes to efficient phagocytosis in macrophages.

show abstract

“…This discrepancy is likely to originate from the use of only the Triton X-100 soluble cell lysate fractions in the prior study. Invasion by fimbriated P. gingivalis thus evokes the formation of integrin-associated focal adhesions and will likely stimulate the cascade of events that normally follows integrin activation (Alrutz & Isberg, 1998;Metheniti et al, 2001;Ozeri et al, 2001;McGee et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Gingival epithelial cell signalling and cytoskeletal responses to Porphyromonas gingivalis invasion

et al. 2003

View full text Add to dashboard Cite

Porphyromonas gingivalis, an oral pathogen, can internalize within primary gingival epithelial cells (GECs) through an invasion mechanism mediated by interactions between P. gingivalis fimbriae and integrins on the surface of the GECs. Fimbriae-integrin-based signalling events were studied by fluorescence microscopy, and the subcellular localization of integrin-associated signalling molecules paxillin and focal adhesion kinase (FAK), and the architecture of the actin and microtubule cytoskeleton were examined. GECs infected with P. gingivalis for 30 min demonstrated significant redistribution of paxillin and FAK from the cytosol to cell peripheries and assembly into focal adhesion complexes. In contrast, a fimbriae-deficient mutant of P. gingivalis did not contribute substantially to activation of paxillin or FAK. After 24 h, the majority of paxillin and FAK had returned to the cytoplasm with significant co-localization with P. gingivalis in the perinuclear region. Wild-type P. gingivalis induced nucleation of actin filaments forming microspike-like protrusions and long stable microfilaments distributed throughout the cells. Fimbriae mutants promoted a rich cortical actin meshwork accompanied by membrane ruffling dispersed along the cell membrane. Remarkable disassembly and nucleation of the actin and microtubule filamentous network was observed following 24 h infection with either wild-type or fimbriae-deficient mutants of P. gingivalis. The results show that fimbriated P. gingivalis cells induce formation of integrin-associated focal adhesions with subsequent remodelling of the actin and tubulin cytoskeleton.

show abstract

Involvement of FAK/Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes

Cited by 37 publications

References 22 publications

Integrin βν-mediated Phagocytosis of Apoptotic Cells in Drosophila Embryos

Integrin βν-mediated Phagocytosis of Apoptotic Cells in Drosophila Embryos

Eps8 Protein Facilitates Phagocytosis by Increasing TLR4-MyD88 Protein Interaction in Lipopolysaccharide-stimulated Macrophages

Gingival epithelial cell signalling and cytoskeletal responses to Porphyromonas gingivalis invasion

Contact Info

Product

Resources

About