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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2004.1
- 수록면
- 172 - 178 (7page)
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초록· 키워드
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Agents that elevate celular cAMP are known to inhibit the activation of phospholipase D (PLD). ylated by cAMP-dependent protein kinase (PKA) and PKA-mediated phosphorylation afects the in-teraction between PLD and RhoA, a membrane regulator of PLD. PLD1, but not PLD2 was found to be phosphorylated in vivo by the treatment of dibutyryl cAMP (dbcAMP) and in vitro by PKA. PKA inhibitor (KT5720) abolished the dbcAMP-in-duced phosphorylation of PLD1, but dibutyryl cGMP (dbcGMP) failed to phosphorylate PLD1. The association between PLD1 and Val14RhoA in an dbcAMP and dbcGMP. Moreover, RhoA but not PLD1 was disociated from the membrane to the cytosolic fraction in dbcAMP-treated cells. These results sugest that both PLD1 and RhoA are phosphorylated by PKA and the interaction bet-wen PLD1 and RhoA is inhibited by the phos-phorylation of RhoA rather than by the phosphor-ylation of PLD1.
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참고문헌 (28)
참고문헌 신청
/ / CyclicAMP-elevating agents block chemoattractant activation ofdiradylglycerol generation by inhibiting phospholipase Dactivation : 3498 ~ 504
/ 1995 / Altshuller YM Engebrecht J : 29640 ~ 3
/ 1995 / Regulation of phospholipase D in HL60 cells : 8466 ~ 73
/ 1996 / Protein kinase A phosphorylationof RhoA mediates the morphological and functional effectsof cyclic AMP in cytotoxic lymphocytes : 510 ~ 9
/ 1997 / Regulation of eukaryoticphosphatidylinositol-specific phospholipase C andphospholipase D : 475 ~ 509
/ 1995 / Altshuller YM Engebrecht J : 29640 ~ 3
/ 1995 / Regulation of phospholipase D in HL60 cells : 8466 ~ 73
/ 1996 / Protein kinase A phosphorylationof RhoA mediates the morphological and functional effectsof cyclic AMP in cytotoxic lymphocytes : 510 ~ 9
/ 1997 / Regulation of eukaryoticphosphatidylinositol-specific phospholipase C andphospholipase D : 475 ~ 509
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