CAMSAP2
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CAMSAP2
Calmodulin-regulated spectrin-associated protein family member 2 (CAMSAP2) is a protein in humans that is encoded by the CAMSAP2 gene. CAMSAP2 possesses a microtubule-binding domain near the C-terminal region where "microtubule interactions" occur. On the C-terminal regions, protein to protein interactions are accelerated by three Coiled coil, coiled-coil domains, which function as molecular spacers. CAMSAP2 acts as a microtubule minus-end anchor and binds microtubules through its CKK domain. CAMSAP2 is necessary for the proper organization and stabilization of interphase microtubules. The protein also plays a role in cell migration. CAMSAP2 stabilizes and attaches microtubule minus ends to the Golgi apparatus, Golgi through the AKAP9 complex and myomegalin. CLASP1 proteins are responsible for microtubule stability which are not required for the Golgi tethering. When no centromeres are present, AKAP9 and CAMSAP-2 dependent pathways of the microtubule minus ends become a dominant for ...
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CAMSAP3
Calmodulin-regulated spectrin-associated protein family member 3 (CAMSAP3) is a human protein encoded by the gene CAMSAP3. The protein is commonly referred to as Nezha. Function CAMSAP3 acts as a minus-end anchor of microtubules, and binds to them through its CKK domain. In epithelial cells Epithelium or epithelial tissue is a thin, continuous, protective layer of cells with little extracellular matrix. An example is the epidermis, the outermost layer of the skin. Epithelial ( mesothelial) tissues line the outer surfaces of man ..., it anchors microtubules to the apical cortex, causing them to grow in an apical-to-basal direction. This gives the epithelial cells their rectangular shape. In other species In early mouse embryogenesis, the interphase bridge linking sister cells is enriched with CAMSAP3. See also * CAMSAP1 * CAMSAP2 References

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