Anti-STX17 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

STX17 also known as Syntaxin 17 is a SNARE protein involved in membrane fusion processes. Its molecular weight is approximately 34 kDa. STX17 is predominantly expressed in the endoplasmic reticulum and associated membranes. The protein plays a mechanical role in mediating the fusion of vesicles with target membranes facilitating the transport of molecules within cells. STX17 localizes mostly in cell types associated with high metabolic activity where it supports cellular trafficking demands.

Biological function summary

Syntaxin 17 contributes to the formation of a multiprotein complex involved in the fusion of autophagosomes with lysosomes. This process is important for macroautophagy where damaged organelles and proteins are degraded and recycled. The protein forms a functional unit with other SNARE proteins including VAMP8 and SNAP29 to carry out its role. It ensures cellular homeostasis by facilitating the clearance of unnecessary or damaged cellular components under stress conditions.

Pathways

Syntaxin 17 is critical in the autophagy and endocytosis pathways. These pathways are involved in the degradation and recycling of cellular components maintaining cellular integrity and energy balance. In the autophagy pathway STX17 functions alongside proteins such as LC3 and Beclin-1 coordinating the recognition and processing of autophagosomes. In the endocytosis pathway its interactions help balance the intake and processing of extracellular materials.

Associated diseases and disorders

STX17 shows significant connections to neurodegenerative disorders and cancer. Its dysfunction in the autophagy process may lead to accumulation of toxic protein aggregates contributing to disorders like Alzheimer's disease. Defects or mutations in the functioning of STX17 have been linked to impaired cellular waste disposal in this context. In cancer alterations in STX17 expression or function can disrupt autophagic processes and affect cancer cell survival. Understanding its link with neurodegenerative proteins such as tau could offer insights for therapeutic strategies.