Haffner C, Takei K, Chen H, Ringstad N, Hudson A, Butler M H, Salcini A E, Di Fiore P P, De Camilli P
Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.
FEBS Lett. 1997 Dec 15;419(2-3):175-80. doi: 10.1016/s0014-5793(97)01451-8.
Synaptojanin 1 is an inositol 5-phosphatase with a putative role in clathrin-mediated endocytosis. Goal of this study was to provide new evidence for this hypothesis. We show that synaptojanin 1 is concentrated at clathrin-coated endocytic intermediates in nerve terminals. Furthermore, we report that synaptojanin-170, an alternatively spliced isoform of synaptojanin 1, binds Eps15, a clathrin coat-associated protein. Binding is mediated by the COOH-terminal region of synaptojanin-170 which we show here to be poorly conserved from rat to humans, but to contain in both species three asparagine-proline-phenylalanine (NPF) repeats. This motif has been found to be the core of the binding site for the EH domains of Eps15. Together with previous data, our results suggest that synaptojanin 1 can be recruited to clathrin-coated pits via a multiplicity of interactions.
突触素1是一种肌醇5-磷酸酶，推测其在网格蛋白介导的内吞作用中发挥作用。本研究的目的是为这一假说提供新证据。我们发现突触素1集中在神经末梢的网格蛋白包被的内吞中间体上。此外，我们报道了突触素1的一种可变剪接异构体突触素-170与Eps15（一种与网格蛋白包被相关的蛋白）结合。结合是由突触素-170的COOH末端区域介导的，我们在此表明该区域从大鼠到人类的保守性较差，但在两个物种中均含有三个天冬酰胺-脯氨酸-苯丙氨酸（NPF）重复序列。已发现该基序是Eps15的EH结构域结合位点的核心。结合先前的数据，我们的结果表明突触素1可通过多种相互作用被招募到网格蛋白包被的小窝中。
