Microtubule-interacting and trafficking domain-containing protein 1 (MITD1)

MITD1 is a **conserved protein** characterized by an N-terminal MIT (microtubule interacting and trafficking) domain and a unique C-terminal phospholipase D-like (PLD-like) domain[1][2]. The protein interacts specifically with a subset of **ESCRT-III complex subunits**, including CHMP1A/B, CHMP2A, CHMP3, CHMP4A/B, CHMP6, and IST1[2][3]. MITD1 is **essential for proper abscission during cytokinesis**, the final step in cell division, by facilitating the recruitment and activity of ESCRT-III complexes at the midbody; its depletion leads to failed cytokinesis, multinucleation, and increased midbody persistence[1][3][4]. Beyond its role in cell division, MITD1 has **antiviral functions**, notably inhibiting replication of flaviviruses by sequestering ESCRT-III components (such as CHMP1B and CHMP4B) in lipid-rich cellular regions, thus interfering with virus-induced membrane remodeling[2]. Unlike some other MIT domain–containing proteins, MITD1 does not appear to have enzymatic PLD activity, serving instead as a structural and regulatory adaptor for ESCRT-III-driven membrane processes[1]. There are currently no known drugs that specifically target MITD1, nor is it a validated therapeutic target or approved biomarker. It is considered a research protein important for understanding cell division and virus–host interactions.

Other names

MIT domain-containing protein 1LOC129531MITmicrotubule-interacting and transport domain-containing 1MITD1