Post-Translationally Modified S12, Absent In Transformed


homology between S12 and eIF3 and TFIIH subunits, coelution with immunoproteasome subunits, and differential posttranslational modification and nuclear localization, these data suggest a differential nuclear function of modified and unmodified S12 in cancer. 2004 Wiley-Liss, Inc. Key words: 19S; proteasome; breast cancer; S12; Rpn8 The ubiquitin-proteasome pathway plays a crucial role in many fundamental biochemical processes, including cell cycle, apoptosis, metabolism, immune response, signal transduction, stressresponse and cell differentiation (see reference for a review). The 26S proteasome, consisting of the 20S proteasome core bound by 19S regulatory particles on either end is responsible for ATPdependent nonlysosomal degradation of ubiquitinated intracellular proteins. Changes in composition or in posttranslational modification of both 20S and 19S subunits can affect the activity of the 26S proteasome complex. Several independent lines of research point to the proteasome

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