PLEKHA7
Description
The PLEKHA7 (pleckstrin homology domain containing A7) is a protein-coding gene located on chromosome 11.
PLEKHA7, or Pleckstrin homology domain-containing family A member 7, is a protein crucial for the stability and integrity of adherens junctions. It was initially discovered while searching for binding partners for p120, a key protein involved in cell-cell adhesion. PLEKHA7 was found to interact with the N-terminal region of p120. It was also independently identified as a protein interacting with the globular head domain of Paracingulin. PLEKHA7 localizes specifically to the zonular adherens junctions in epithelial cells. The structure of PLEKHA7 is characterized by two WW domains followed by a Pleckstrin homology domain (PH) in the N-terminal region. The C-terminal half contains three coiled coil (CC) domains and two Proline-rich (Pro) domains. PLEKHA7 exists in different isoforms, with two major isoforms of 135 kDa and 145 kDa found in various tissues, including colon, liver, lung, eye, pancreas, kidney, and heart. Additionally, two major transcripts of 5.5 kb and 6.5 kb have been identified in brain, kidney, liver, small intestine, placenta, and lung, while only one PLEKHA7 mRNA transcript of 5.5 kb is found in heart, brain, colon, and skeletal muscle.
PLEKHA7 is essential for the formation and stability of zonula adherens junctions. It interacts with CAMSAP3, a protein that anchors microtubules to these junctions, leading to the recruitment of KIFC3 kinesin. This interaction ensures the proper positioning of microtubules at the junctions. PLEKHA7 also plays a role in the docking of ADAM10, a protease involved in cell signaling, to zonula adherens through its interaction with TSPAN33 and PDZD11.
PLEKHA7 is also known as -.
