Recombinant Human DSTN protein (His tag C-Terminus)

Supplementary information

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

DSTN also known as destrin or actin depolymerizing factor is an actin-binding protein with a relatively low molecular mass of approximately 19 kDa. DSTN plays a significant role in actin filament dynamics by enhancing the disassembly of actin filaments into monomeric actin components thereby regulating cytoskeleton organization. The protein is present in a wide range of tissues including the brain and skeletal muscles indicating its importance in various physiological processes.

Biological function summary

DSTN regulates actin cytoskeleton remodeling impacting cell shape and motility. It acts by binding to actin enhancing the turnover and dismantling of actin filaments which is critical for maintaining cellular architecture. DSTN is not known to be part of a larger protein complex but it interacts with other actin-related proteins to exert its function efficiently. Its role in cell movement and structure integrates it into larger cellular processes such as cell division migration and potentially signal transduction.

Pathways

Cytoskeletal rearrangement and cell motility highlight the involvement of DSTN. DSTN associates closely with the Rho and Rac signaling pathways pivotal for cytoskeletal changes and cell division processes. Through these pathways DSTN contributes to modulating cellular responses by interacting with proteins like cofilin another actin-binding protein. This interaction with signaling pathways highlights DSTN's broader influence on cellular functions.

DSTN has an association with neurodegenerative diseases and cancer progression. Aberrations in its activity can result in cytoskeletal dysfunctions to which disorders such as Alzheimer’s disease relate due to the importance of cytoskeletal integrity in neuron function. Additionally DSTN's involvement in cell motility links it to cancer metastasis where unchecked cell movement promotes tumor spread. In these diseases DSTN collaborates mutably with the tau protein and other cytoskeletal regulators highlighting DSTN's relevance in pathological conditions.