Anti-SPAK (phospho S309) antibody

Supplementary info

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

Activity summary

SPAK also known as Ste20-related Proline-Alanine-rich Kinase is a serine/threonine protein kinase with a molecular mass of approximately 61 kDa. It plays a critical mechanical role in the regulation of ion transport and cell volume by phosphorylating a variety of ion transporters and channels. SPAK expresses in many tissues including the kidney brain and heart which highlights its multifaceted functions in different physiological contexts.

Biological function summary

SPAK integrates into cellular signaling processes by contributing to the regulation of sodium potassium and chloride transport. This kinase mainly interacts within complexes of kinase networks that include OSR1 and WNK kinases. SPAK has essential roles in mediating responses to osmotic stress and modulating ion homeostasis reflecting its participation in regulating blood pressure and neuronal excitability.

Pathways

SPAK serves a significant role in the WNK signaling pathway and the MAPK pathway. WNK kinases activate SPAK through phosphorylation allowing SPAK to modulate the activity of co-transporter proteins. This interaction is important for managing ion fluxes across membranes. Furthermore SPAK's interplay with the MAPK pathway implicates it in cellular stress responses and proliferation where it coordinates with players like p38 MAPK to influence cell survival.

Associated diseases and disorders

Researchers have linked SPAK to conditions like hypertension and epilepsy. Its association with hypertension arises through its involvement in sodium balance where disrupted SPAK activity can lead to increased blood pressure. SPAK also connects with epilepsy via modulation of neuronal ion transport playing a part alongside other proteins such as OSR1 in maintaining neuronal excitability. Understanding SPAK's role helps in developing strategies for managing these conditions.