Disease relevance of STRAP

• Molecular cloning and characterization of human MAWD, a novel protein containing WD-40 repeats frequently overexpressed in breast cancer [1].
• Oncogenic Serine-Threonine Kinase Receptor-Associated Protein Modulates the Function of Ewing Sarcoma Protein through a Novel Mechanism [2].
• Strap remains localized in the cytoplasm in cells derived from ataxia telangiectasia individuals with defective ATM, as well as in cells expressing a Strap mutant that cannot be phosphorylated by ATM [3].
• METHODS: Strap muscle neurovascular supply was studied in 16 cadavers, including one transparent corrosion cast specimen with injected vessels [4].
• INTERVENTIONS: The braces studied were the Count'R-Force Tennis Elbow Brace, the Body Glove Airprene Elbow Support, and a placebo brace that consisted of a modified DePuy Levy Clinic Patella Strap [5].

High impact information on STRAP

• We report a cofactor in the p300 coactivator complex, Strap, which has an unusual structure, being composed almost entirely of a tandem series of six tetratricopeptide repeat (TPR) motifs [6].
• ATM phosphorylates Strap at a serine residue, stabilizing nuclear Strap and facilitating formation of a stress-responsive co-activator complex [3].
• Here we report a new pathway in which ATM kinase signals the DNA damage response by targeting the transcriptional cofactor Strap [3].
• In the latter case, unrip is recruited to the active SMN complex via a stable interaction with Gemin7 [7].
• Our data identify unrip as the first component of the U snRNP assembly machinery that associates with the SMN complex in a compartment-specific way [7].

Biological context of STRAP

• Using a conventional two-hybrid technique with MAWD as bait protein, a novel full-length cDNA was isolated and sequenced from a human liver cDNA library [8].
• Targeting Strap to the nucleus reinstates protein stabilization and activates the DNA damage response [3].
• These results indicate that the nuclear accumulation of Strap is a critical regulator in the damage response, and argue that this function can be assigned to ATM through the DNA damage-dependent phosphorylation of Strap [3].

Anatomical context of STRAP

• In the cytoplasm, a macromolecular complex containing the survival motor neuron (SMN) protein, Gemin2-8 and Unrip mediates the ATP-dependent assembly of Sm proteins and snRNAs into snRNPs [9].

Other interactions of STRAP

• Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein [10].
• We have previously identified a WD domain-containing protein, serine-threonine kinase receptor-associated protein (STRAP), which inhibits transforming growth factor beta (TGF-beta) signaling through interaction with receptors and Smad7 and promotes growth and enhances tumorigenicity [2].

References