Abstract
Purpose of Review
Here we review the molecular organization and protein–protein interactions of the following plaque proteins of tight junction (TJ): MAGI-1, -2 and -3, the polarity complex Par3/Par6/aPKC, afadin, MUPP1, PATJ, Pals1, cingulin, paracingulin, and JEAP. We analyze the status of these proteins in cancer tissue and their association to tumor suppressor proteins, kinases, and viral oncoproteins. Zonula occludens plaque proteins of the TJ are discussed separately in the preceding review within this issue.
Recent Findings
The expression of the above-mentioned TJ plaque proteins is frequently altered in cancer. However, while the loss of some of these proteins correlates with cancer development and low sensitivity to apoptosis, the overexpression of others is associated with poor patient survival rates. Some of these proteins are associated with tumor suppressor proteins like PTEN or to kinases activated in cancer like Src, while others are the target of oncoviral proteins or interact with signaling pathways involved in cell proliferation and transformation.
Summary
TJ present at the apical junctional complex of epithelial cells control the passage of ions and molecules through the paracellular route and block the movement of proteins and lipids within the plasma membrane from the apical to the basolateral surfaces. TJ are constituted by integral proteins linked to a vast group of plaque proteins, which form a scaffold associated with the actomyosin cytoskeleton. In cancerous tissues some of these plaque proteins are silenced while others are overexpressed.
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