Dubois T, Oudinet J P, Mira J P, Russo-Marie F
INSERM U 332, Institut Cochin de Génétique Moléculaire (ICGM), Paris, France.
Biochim Biophys Acta. 1996 Oct 11;1313(3):290-4. doi: 10.1016/0167-4889(96)00102-4.
Annexins and protein kinases C belong to two distinct families of ubiquitous cytoplasmic proteins involved in signal transduction. All annexins share the property of binding calcium and phospholipids in the presence of calcium. Protein kinases C belong to three distinct groups of kinases: cPKCs (conventional PKCs) depend on calcium, diacylglycerol and negatively charged phospholipids for their activity, nPKCs (novel PKCs) depend on diacylglycerol and negatively charged phospholipids and aPKCs (atypical PKCs) only require negatively charged phospholipids. Almost all annexins are both in vitro and in vivo substrates for PKCs except annexin V. All annexins have a putative binding site for PKCs but only annexin V would possess a potential pseudo-substrate site. We propose that annexin V modulates the activity of some cPKCs on their substrates which may be the other annexins.
膜联蛋白和蛋白激酶C属于参与信号转导的两类不同的普遍存在的细胞质蛋白家族。所有膜联蛋白都具有在钙离子存在下结合钙和磷脂的特性。蛋白激酶C属于三类不同的激酶:传统蛋白激酶C(cPKCs)的活性依赖于钙、二酰基甘油和带负电荷的磷脂,新型蛋白激酶C(nPKCs)依赖于二酰基甘油和带负电荷的磷脂,非典型蛋白激酶C(aPKCs)仅需要带负电荷的磷脂。除膜联蛋白V外,几乎所有膜联蛋白在体外和体内都是蛋白激酶C的底物。所有膜联蛋白都有一个假定的蛋白激酶C结合位点,但只有膜联蛋白V会拥有一个潜在的假底物位点。我们提出,膜联蛋白V可调节某些传统蛋白激酶C对其底物(可能是其他膜联蛋白)的活性。