Promyelocytic leukemia protein

Promyelocytic leukemia protein (PML) is a tumor suppressor protein that in humans is encoded by the PML gene.

Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies (Nuclear dots) where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.

Interactions

Promyelocytic leukemia protein has been shown to interact with:

• ANKRD2,
• CREB-binding protein,
• Cyclin T1,
• Death associated protein 6,
• GATA2,
• HDAC1,
• HDAC3,
• HHEX,
• MAPK11,
• MYB,
• Mdm2,
• Nerve Growth factor IB,
• Nuclear receptor co-repressor 1,
• Nuclear receptor co-repressor 2,
• P53,
• RPL11,
• Retinoblastoma protein,
• Retinoic acid receptor alpha,
• SIN3A,
• SKI protein,
• STAT3,
• Serum response factor and
• Small ubiquitin-related modifier 1,
• Sp1 transcription factor,
• TOPBP1,
• Thymine-DNA glycosylase, and
• Zinc finger and BTB domain-containing protein 16.

See also

• RING finger domain

External links

• PML protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)