Tripartite motif containing 44 (TRIM44)

Tripartite motif containing 44 (TRIM44) is a member of the TRIM protein family, distinguished by its conserved domains including zinc finger, B-box, coiled-coil, and glutamate-rich regions[1][2]. Unlike canonical TRIM proteins, TRIM44 lacks a RING domain, separating it from classic E3 ligases; however, it functions as a deubiquitinase and protein quality control factor[2]. TRIM44 links the ubiquitin-proteasome system with autophagy by promoting SQSTM1/p62 oligomerization, supporting the removal of misfolded or aggregated proteins through targeting them for autophagic degradation[1]. It is upregulated in multiple myeloma and other aggregate-prone diseases, where it can promote cell survival and pathological changes such as bone destruction[1]. TRIM44 also plays a role in DNA damage response by interacting with PARP1 and the ATM/MRN complex, dictating cell sensitivity to PARP inhibitors and coordinating double-strand break repair[2]. Thus, TRIM44 is a multifunctional regulatory protein at the crossroads of proteostasis, autophagy, and DNA repair, making it a candidate therapeutic target in cancers and neurodegenerative diseases.

Other names

TRIM44Tripartite motif protein 44

Modulation of autophagy and proteasome pathway activity; Regulation of DNA damage response signaling via PARP1 and ATM/MRN complex; Promotion of SQSTM1/p62 oligomerization and aggregate clearance; Influencing cell sensitivity/resistance to proteasome and PARP inhibition.