Longin Sari, Jordens Jan, Martens Ellen, Stevens Ilse, Janssens Veerle, Rondelez Evelien, De Baere Ivo, Derua Rita, Waelkens Etienne, Goris Jozef, Van Hoof Christine
Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium.
Biochem J. 2004 May 15;380(Pt 1):111-9. doi: 10.1042/BJ20031643.
We have described recently the purification and cloning of PP2A (protein phosphatase 2A) leucine carboxylmethyltransferase. We studied the purification of a PP2A-specific methylesterase that co-purifies with PP2A and found that it is tightly associated with an inactive dimeric or trimeric form of PP2A. These inactive enzyme forms could be reactivated as Ser/Thr phosphatase by PTPA (phosphotyrosyl phosphatase activator of PP2A). PTPA was described previously by our group as a protein that stimulates the in vitro phosphotyrosyl phosphatase activity of PP2A; however, PP2A-specific methyltransferase could not bring about the activation. The PTPA activation could be distinguished from the Mn2+ stimulation observed with some inactive forms of PP2A, also found associated with PME-1 (phosphatase methylesterase 1). We discuss a potential new function for PME-1 as an enzyme that stabilizes an inactivated pool of PP2A.
我们最近描述了PP2A(蛋白磷酸酶2A)亮氨酸羧甲基转移酶的纯化和克隆。我们研究了与PP2A共纯化的一种PP2A特异性甲酯酶的纯化过程,发现它与PP2A的无活性二聚体或三聚体形式紧密相关。这些无活性的酶形式可被PTPA(PP2A的磷酸酪氨酸磷酸酶激活剂)重新激活为丝氨酸/苏氨酸磷酸酶。我们小组之前将PTPA描述为一种刺激PP2A体外磷酸酪氨酸磷酸酶活性的蛋白质;然而,PP2A特异性甲基转移酶无法实现激活。PTPA激活与一些也与PME-1(磷酸酶甲酯酶1)相关的无活性形式的PP2A所观察到的Mn2+刺激不同。我们讨论了PME-1作为一种稳定PP2A失活库的酶的潜在新功能。