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Tetratricopeptide repeat domain 28 (TTC28) is a large (271 kDa) scaffold protein containing multiple tetratricopeptide repeat (TPR) domains that facilitate protein-protein interactions, particularly during cell division[1][2][8]. TTC28 is essential for the regulation of mitosis and cytokinesis by organizing spindle midzone microtubules and midbody formation, processes crucial for proper cell division[2][7][8]. It interacts with HSPA8 and LAMP2A, serving as a substrate for chaperone-mediated autophagy, and is rapidly degraded via this pathway[1][3]. Loss or mutation of TTC28 leads to chromosomal instability, which is a hallmark of cancer and may sensitize cancer cells to drugs that inhibit mitosis and cytokinesis[1][3]. TTC28 is not classified as a conventional therapeutic target like a receptor or enzyme, but is increasingly recognized for its role in maintaining genome integrity and as a potential biomarker or research target in oncology[1][5][3].
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