Recombinant Human Profilin 1 protein

Supplementary information

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

Profilin 1 also known as Profilin-1 or Profilin is a small actin-binding protein with a molecular weight of approximately 15 kDa. It is expressed across various tissues including muscle brain and epithelial cells. Profilin 1 interacts with monomeric actin (G-actin) to regulate actin polymerization by binding to actin monomers. This protein also interacts with polyphosphoinositides and proline-rich sequences playing a mechanical role in balancing actin filament assembly and disassembly.

Biological function summary

Profilin 1 acts as an important regulator of the cytoskeleton facilitating cellular processes like motility and division. It participates in the formation of actin filaments by delivering actin monomers to barbed ends promoting polymerization. Profilin 1 is part of the complex that controls actin dynamics and this ability to modulate actin structure allows it to influence cell shape and internal movement. The protein's interactions help support the actin cytoskeleton for intracellular trafficking and signal transduction.

Pathways

Profilin 1 has important roles in the regulation of the actin cytoskeleton and Rho signaling pathways. These pathways are important in cell migration and adhesion. During cellular processes Profilin 1's interactions with actin and polyphosphoinositides link it to other proteins such as Rho GTPases which are associated with cytoskeletal dynamics. Profilin 1 can influence these pathways by modulating actin dynamics and interacting with proteins involved in these signaling cascades.

Disruptions in Profilin 1 function are linked to neurodegenerative diseases and cancer metastasis. For example aberrant Profilin 1 activity can contribute to amyotrophic lateral sclerosis (ALS) by affecting neuronal structure and transport. Dysregulation of its interaction with actin or polyphosphoinositides might also lead to enhanced cancer cell migration and invasion. It may interact with other proteins implicated in these diseases such as the ALS-related protein TDP-43 or cancer-related kinases making it significant in understanding these conditions.