SPRED1 Human

SPRED1 contains an EVH1 (Ena/VASP Homology 1) domain, which is crucial for its interaction with other proteins. The EVH1 domain allows SPRED1 to bind to proline-rich sequences in target proteins, facilitating its role in cellular signaling pathways . SPRED1 acts as a negative regulator of the Ras/MAPK (Mitogen-Activated Protein Kinase) signaling pathway, which is essential for cell proliferation and differentiation .

SPRED1 is phosphorylated by tyrosine kinases in response to several growth factors. It can function as a homodimer or as a heterodimer with SPRED2 to regulate the activation of the MAP kinase cascade . This regulation is vital for maintaining cellular homeostasis and preventing uncontrolled cell growth, which can lead to cancer .

Mutations in the SPRED1 gene are associated with several diseases, including Legius Syndrome and Neurofibromatosis type 1-like syndrome (NFLS) . Legius Syndrome is characterized by multiple café-au-lait spots on the skin, freckling, and learning disabilities . NFLS shares some clinical features with Neurofibromatosis type 1 but is generally considered to be a milder condition .

The recombinant form of SPRED1 is used in research to study its role in cellular signaling and its potential as a therapeutic target. By understanding how SPRED1 regulates the Ras/MAPK pathway, researchers hope to develop new treatments for diseases associated with dysregulation of this pathway, such as cancer .