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Example sentences for: odc
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The best-characterized example of ubiquitin-independent degradation is the degradation of ornithine decarboxylase (ODC), which is dependent upon ODC interaction with the targeting protein antizyme (Az) [ 18 ] . How ubiquitinated substrates or Az-bound ODC is recognized by the 26S proteasome is not well understood.
The cell surface expressed integrins can control this process by physically interacting with the extracellular matrix proteins and other cell surface proteins on endothelial cells lining the blood vessel wall [ 1 ] . These integrins signal adhesion and migration by communicating with several tyrosine kinases inside the cell, including the Focal Adhesion Kinase (FAK) and Src family kinases [ 1 2 ] . Src kinases control the activation of FAK, as well as the tyrosine phosphorylation of critical substrates that regulate adhesion and migration [ 3 ] . Indeed, colon cancer cells with high metastatic potential have elevated levels of Src activity or activating mutations in the Src gene [ 4 5 ] . One Src substrate that is involved in regulating an important signaling node in this process is the adaptor protein p130 cas (Cas) [ 6 7 8 9 10 ] . Cas appears to play a central role in the transformation process by several oncogenes including ras, ornithine decarboxylase (ODC), v-Src, v-crk, and Bcr-Abl, as these tumors all have elevated levels of tyrosine phosphorylated Cas [ 6 11 12 13 ] . Cells from mice that lack Cas have much reduced migration and are resistant to transformation by v-Src, while expression of Cas anti-sense RNA in cells transformed with ras, v-Src or ODC result in reversion of the transformed phenotype [ 11 14 15 ] . Furthermore, increased expression of Cas can rescue cell migration and adhesion in cells expressing the tumor suppressor PTEN, and can enhance cell migration and adhesion in normal cells, with a major role being played by the substrate domain [ 16 17 ] .
The 26S proteasome is responsible for the bulk turnover of cytoplasmic and nuclear proteins in eukaryotic cells and also plays a key role in the regulation of cell cycle, signal transduction, transcription as well as antigen presentation [ 17 18 19 20 21 ] . Most of the known proteasomal substrates are marked and targeted to proteasome by ubiquitination [ 17 19 20 ] . Ubiquitination, however, is not an obligatory step for substrate targeting to proteasome [ 17 18 20 ] . The degradation of the ornithine decarboxylase (ODC), the rate-limiting enzyme for polyamine synthesis, involves a protein named antizyme (Az), which binds and targets ODC to 26S proteasome for degradation [ 18 ] . However, ODC has remained an "orphan" in Az-dependent proteasomal degradation.
This suggests the existence of a novel BMP-regulated "conditional" targeting activity of Az that is distinct from the constitutive targeting activity of Az towards ODC.
SNIP1 and ODC exhibited similar affinity to Az in the yeast two-hybrid test (Fig.
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