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Fig. 2. | Molecular Medicine

Fig. 2.

From: The Chediak-Higashi Protein Interacts with SNARE Complex and Signal Transduction Proteins

Fig. 2.

Interactions of LYST with proteins that regulate vesicle docking and fusion in exocytosis. Not all salient interactions are shown (e.g., synaptotagmin also interacts with syntaxin; syntaxin is phosphorylated by CALMK2). According to this hypothesis, LYST binds to HRS, modifying HRS-mediated modulation of SNAP25, a component of the tSNARE-vSNARE docking complex. LYST also binds to CALM, bringing Ca2+ into the proximity of HRS, inhibiting HRS binding to SNAP25. Docking leads to transient opening of Ca2+channels, and Ca2+-CALM complexes activate membrane fusion. LYST interacts with 14-3-3 and CK2, which modify activity of several proteins of the tethering, docking, and fusion machinery.

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