Interaction with a kinesin-2 tail propels choline acetyltransferase flow towards synapse.
Interaction with a kinesin-2 tail propels choline acetyltransferase flow towards synapse.
复制标题
与驱动蛋白 2 尾部的相互作用推动胆碱乙酰转移酶流向突触。
DOI：
10.1111/j.1600-0854.2012.01361.x
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Ray,Krishanu
中科院分区：
文献类型：
--
作者：
Sadananda,Aparna;Hamid,Runa;Doodhi,Harinath;Ghosal,Debnath;Girotra,Mukul;Jana,SwadhinChandra;Ray,Krishanu
Bulk flow constitutes a substantial part of the slow transport of soluble proteins in axons. Though the underlying mechanism is unclear, evidences indicate that intermittent, kinesin‐based movement of large protein‐aggregates aids this process. Choline acetyltransferase (ChAT), a soluble enzyme catalyzing acetylcholine synthesis, propagates toward the synapse at an intermediate, slow rate. The presynaptic enrichment of ChAT requires heterotrimeric kinesin‐2, comprising KLP64D, KLP68D and DmKAP, inDrosophila. Here, we show that the bulk flow of a recombinant Green Fluorescent Protein‐tagged ChAT (GFP::ChAT), inDrosophilaaxons, lacks particulate features. It occurs for a brief period during the larval stages. In addition, both the endogenous ChAT and GFP::ChAT directly bind to the KLP64D tail, which is essential for the GFP::ChAT entry and anterograde flow in axon. These evidences suggest that a direct interaction with motor proteins could regulate the bulk flow of soluble proteins, and thus establish their asymmetric distribution.
