MARCKS: Difference between revisions
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Latest revision as of 17:58, 17 March 2025
Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) is a protein that plays a crucial role in cellular processes, including cell motility, secretion, and membrane trafficking. It is encoded by the MARCKS gene in humans. As a major substrate for protein kinase C (PKC), MARCKS is involved in the regulation of the actin cytoskeleton, contributing to the dynamic changes required for cell movement and shape alterations.
Function[edit]
MARCKS is a widely expressed protein that participates in various cellular functions. Its primary mechanism of action involves the regulation of the cytoskeleton, an internal framework of cells composed of actin filaments. MARCKS achieves this by binding to actin filaments and calmodulin, a calcium-binding messenger protein, thereby influencing cell motility and morphology. Additionally, MARCKS plays a role in the exocytosis process, where it is implicated in the secretion of neurotransmitters and other molecules from cells.
The protein contains a unique domain known as the PSD-95/Dlg/ZO-1 (PDZ) binding motif, which allows it to interact with other proteins and participate in signaling pathways. The phosphorylation of MARCKS by PKC leads to its detachment from the membrane, a process that is crucial for its function in cell signaling and membrane trafficking.
Clinical Significance[edit]
Alterations in MARCKS expression and function have been associated with several diseases, including cancer, neurological disorders, and cardiovascular diseases. In cancer, overexpression of MARCKS has been observed in various types, suggesting a role in tumor progression and metastasis. In the nervous system, MARCKS is involved in neuronal development and is essential for brain function, with implications in diseases such as Alzheimer's disease.
Research[edit]
Research on MARCKS continues to uncover its multifaceted roles in cellular processes and disease mechanisms. Studies have focused on understanding how MARCKS interacts with other proteins and signaling pathways, with the aim of developing therapeutic strategies targeting its function in diseases.
See Also[edit]
References[edit]
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