생명과학회지 (Journal of Life Science)

  • 제15권3호
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  • Pages.492-498
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  • 2005
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  • 1225-9918(pISSN)
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  • 2287-3406(eISSN)
한국생명과학회 (Korean Society of Life Science)
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Activation of Phospholipase D2 through Phosphorylation of Tyrosine-470 in Antigen-stimulated Mast Cells

  • 발행 : 2005.06.01
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초록

PLDI 활성화 기전은 여러 보고가 있으나 PLD2 활성화에 대한 기전은 아직 연구의 대상이다. RBL-2H3 비만세포에서 HA-PLD2의 인산화 가능한 타이로신 잔기를 점돌연변이 시킨 DNA플라즈미드를 이용하여 11번, 14번, 470번의 타이로신이 항원자극에 의해 인산화 됨을 알아냈고 특히 470번 타이로신의 인산화가 PLD2 활성화에 중요하다는 결과를 얻었다.

The mechanism of activation of phospholipase D2 (PLD2) remains undefined although mechanisms have been described for the activation of PLDI. By expression of mutated forms of haemaglutinnin-tagged PLD2 in a mast cell (RBL-2H3) line, we show that PLD2 is phosphorylated at tyrosines -11, -14, and -470 and that tyrosine-470 is critical for activation of PLD2 by antigen. Studies were performed with mutated-DNA constructs for haemaglutinnin-tagged PLD2 in which codons for tyrosine -11, -14, -165, and -470 were mutated to phenylalanine either individually or collectively. Transient expression of these constructs showed that mutation of tyrosine -11, -14, -470, or all tyrosines (all-mutated PLD2) suppressed antigen-induced tyrosine phosphorylation of PLD2 but only the tyrosine-470 mutant failed to be activated by antigen as assessed by in vitro assay of immunoprepitated PLD2 or by assay of PLD in intact cells. The critical role of tyrosine-470 was confirmed in studies with add-back mutants (phenylalanine back to tyrosine) of the all-mutated PLD. The findings provide the first description of a mechanism of activation of PLD2 in a physiological setting.

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참고문헌

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