TATA element modulatory factor 1 (TMF1)

TATA element modulatory factor 1 (TMF1) is a multifunctional protein acting as both a **Golgi-associated tethering factor** and a **nuclear transcriptional co-regulator**[1][2][5][7]. In the cytosol, TMF1 helps maintain Golgi apparatus integrity and mediates vesicle tethering, especially in **RAB6-dependent retrograde transport** between endosomes, the Golgi apparatus, and the endoplasmic reticulum. TMF1 interacts with multiple Rab GTPases and components of the COG (conserved oligomeric Golgi) complex, facilitating vesicle membrane fusion and cargo sorting[2]. In the nucleus, TMF1 functions as a **transcriptional coactivator**, particularly for the androgen receptor, and regulates transcription by RNA polymerase II. It promotes the ubiquitination and proteasomal degradation of specific transcription factors, notably **STAT3** and **p65/RelA**, thereby modulating gene expression programs related to **angiogenesis, apoptosis, and cell cycle control**[2][5][7]. TMF1 can also form inducible complexes with proteins such as FER kinase and PDGFRβ, influencing chromatin remodeling and expression of cell cycle regulators. TMF1 is thus implicated in several diseases, including certain cancers (by modulating proangiogenic genes), some genetic skeletal disorders, and rare immunodeficiencies involving aberrant gene insertions. There is currently no evidence that TMF1 is a direct therapeutic target for small molecules or biologics, and no drugs directly targeting TMF1 are reported in major curated databases[1][2][5].

Other names

TMFARA160Androgen receptor coactivator 160 kDa proteinAndrogen receptor-associated protein of 160 kDaTATA element modulatory factorandrogen receptor coactivator 160 kDa proteinandrogen receptor-associated protein of 160 kDa