SNPH Human

Syntaphilin is a neuron-specific protein encoded by the SNPH gene in humans. It plays a crucial role in the regulation of mitochondrial dynamics and synaptic function. Syntaphilin is known for its ability to inhibit the formation of the SNARE complex by binding to free syntaxin-1, thereby controlling synaptic vesicle docking and fusion .

Recombinant human syntaphilin is typically produced using bacterial expression systems, such as Escherichia coli (E. coli). The gene encoding syntaphilin is cloned into an expression vector, which is then introduced into the bacterial cells. The bacteria are cultured under conditions that induce the expression of the recombinant protein. After sufficient growth, the cells are harvested, lysed, and the recombinant protein is purified using affinity chromatography techniques. The purified protein often includes a His-tag to facilitate purification and detection .

Syntaphilin’s primary function involves its interaction with mitochondrial and cytoskeletal components. It acts as a static anchor for mitochondria in axons by binding to microtubules, thereby regulating mitochondrial mobility. This interaction is crucial for maintaining proper mitochondrial distribution within neurons, which is essential for neuronal function and energy homeostasis .

Additionally, syntaphilin undergoes post-translational modifications, such as ubiquitination, which regulate its function. Ubiquitination of syntaphilin by the E3 ligase CHIP on specific lysine residues (Lys111 and Lys153) anchors syntaphilin on tubulin, inhibiting mitochondrial motility and promoting mitochondrial dynamics . This regulation is vital for controlling mitochondrial trafficking and tumor cell motility, highlighting syntaphilin’s role in cellular processes beyond neuronal function .