PDCD4

Domain

Binds EIF4A1 via both MI domains.

Function

Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity).

Post-translational modifications

Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation.

Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.

Sequence similarities

Belongs to the PDCD4 family.

Tissue specificity

Up-regulated in proliferative cells. Highly expressed in epithelial cells of the mammary gland. Reduced expression in lung cancer and colon carcinoma.

Cellular localization

• Nucleus
• Cytoplasm
• Shuttles between the nucleus and cytoplasm (By similarity). Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (PubMed:16357133).

Alternative names

• Programmed cell death protein 4
• Neoplastic transformation inhibitor protein
• Nuclear antigen H731-like
• Protein 197/15a
• H731
• PDCD4

Database links

• entrezGene:27250
• omim:608610
• swissprot:Q53EL6

Target type

Proteins

Molecular weight

51735Da