Recombinant Human MOS protein (GST tag N-Terminus)

Supplementary information

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

The MOS protein also known simply as MOS is a serine/threonine-protein kinase with a mass of approximately 39 kDa. It is particularly expressed in oocytes and is an essential component during oocyte maturation. MOS acts mechanically by regulating the transition from meiotic prophase to metaphase and ensures the metaphase arrest which is important for successful fertilization. It is well-conserved across species including in the commonly studied 'mos mouse' model which facilitates detailed exploration of its functions.

Biological function summary

The MOS protein plays a significant role in the regulation of the meiotic cell cycle. It is part of the Mos-MAPK pathway where it activates MAP kinase (MAPK) to propagate signals that stabilize cell division processes in oocytes. MOS ensures the correct timing of progression through meiosis impacting the fidelity and viability of the mature eggs. It forms a complex with other proteins such as MAPK and MEK for effective signal transduction during oocyte maturation.

Pathways

MOS integrates into the mitogen-activated protein kinase (MAPK) signaling pathway which is pivotal for cell cycle regulation in oocytes. The protein is closely related to MEK1 and MAPK which together construct the MAPK cascade leading to activation of key meiotic processes. This cascade also influences the stabilization of cyclin B-CDK1 another intricate player in cell cycle control linking MOS to broader regulatory networks in cell cycle checkpoint regulation.

MOS shows potential involvement in conditions related to infertility and reproductive dysfunction. Aberrant expression or mutation of MOS can disrupt normal meiotic processes leading to failed oocyte maturation and infertility. The protein is also connected to disorders involving inappropriate MAPK pathway activation which can lead to oncogenesis. In particular abnormal interaction with proteins like MEK1 and MAPK may contribute to the pathophysiology of certain cancers where dysregulation of cell division pathways is a hallmark.