Vinculin and Rab5 complex is requited for uptake of Staphyrococcus aureus and interleukin-6 expression

Makoto Hagiwara, Eitoyo Kokubu, Shinsuke Sugiura, Toshinori Komatsu, Hiroyuki Tada, Ryutaro Isoda, Naomi Tanigawa, Yoshiko Kato, Naoyuki Ishida, Kaoru Kobayashi, Misako Nakashima, Kazuyuki Ishihara, Kenji Matsushita

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17 Citations (Scopus)


Vinculin, a 116-kDa membrane cytoskeletal protein, is an important molecule for cell adhesion; however, little is known about its other cellular functions. Here, we demonstrated that vinculin binds to Rab5 and is required for Staphylococcus aureus (S. aureus) uptake in cells. Viunculin directly bound to Rab5 and enhanced the activation of S. aureus uptake. Overexpression of active vinculin mutants enhanced S. aureus uptake, whereas over-expression of an inactive vinculin mutant decreased S. aureus uptake. Vinculin bound to Rab5 at the N-terminal region (1-258) of vinculin. Vinculin and Rab5 were involved in the S. aureus-induced phosphorylation of MAP kinases (p38, Erk, and JNK) and IL-6 expression. Finally, vinculin and Rab5 knockdown reduced infection of S. aureus, phosphorylation of MAPKs and IL-6 expression in murine lungs. Our results suggest that vinculin binds to Rab5 and that these two molecules cooperatively enhance bacterial infection and the inflammatory response.

Original languageEnglish
Article numbere87373
JournalPLoS ONE
Issue number1
Publication statusPublished - 2014 Jan 23


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