Zhou Xiaolai, Sullivan Peter M, Sun Lirong, Hu Fenghua
Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.
J Neurochem. 2017 Oct;143(2):236-243. doi: 10.1111/jnc.14110. Epub 2017 Aug 4.
The frontotemporal lobar degeneration (FTLD) protein progranulin (PGRN) is essential for proper lysosomal function. PGRN localizes in the lysosomal compartment within the cell. Prosaposin (PSAP), the precursor of lysosomal saposin activators (saposin A, B, C, D), physically interacts with PGRN. Previously, we have shown that PGRN and PSAP facilitate each other's lysosomal trafficking. Here, we report that the interaction between PSAP and PGRN requires the linker region of saposin B and C (BC linker). PSAP protein with the BC linker mutated, fails to interact with PGRN and deliver PGRN to lysosomes in the biosynthetic and endocytic pathways. On the other hand, PGRN interacts with PSAP through multiple granulin motifs. Granulin D and E bind to PSAP with similar affinity as full-length PGRN. Read the Editorial Comment for this article on page 154.
额颞叶变性(FTLD)蛋白原颗粒蛋白(PGRN)对正常的溶酶体功能至关重要。PGRN定位于细胞内的溶酶体区室。溶酶体激活剂(鞘脂激活蛋白A、B、C、D)的前体prosaposin(PSAP)与PGRN发生物理相互作用。此前,我们已经表明PGRN和PSAP相互促进彼此的溶酶体运输。在此,我们报告PSAP与PGRN之间的相互作用需要鞘脂激活蛋白B和C的连接区(BC连接区)。BC连接区发生突变的PSAP蛋白无法与PGRN相互作用,也无法在生物合成和内吞途径中将PGRN递送至溶酶体。另一方面,PGRN通过多个颗粒蛋白基序与PSAP相互作用。颗粒蛋白D和E与PSAP结合的亲和力与全长PGRN相似。阅读第154页上关于本文的编辑评论。