High impact information on STP2

• The processing of Stp1p/Stp2p occurs independently of proteasome function and without the apparent involvement of additional components [1].
• In this study, we report that Asi1 is an integral component of the inner nuclear membrane that maintains the latent characteristics of unprocessed Stp1 and Stp2 [2].
• Stp1 and Stp2 are homologous transcription factors in yeast that are synthesized as latent cytoplasmic precursors with NH2-terminal regulatory domains [2].
• A novel genetic screen, specifically designed to search for rare mutations that affect the SPS-sensing pathway, identified the F-box protein Grr1p as an obligatory factor required for Stp1p/Stp2p processing [3].
• We tested one novel motif prediction of the algorithm and found it to be the binding site of Stp2; it is significantly different from the previously predicted Stp2 binding site [4].

Biological context of STP2

• We present evidence that the zinc-finger proteins Stp1p and Stp2p bind directly to the BAP2 promoter [5].

Associations of STP2 with chemical compounds

• Under the given conditions there appears to be only one pathway for induction with L-citrulline, and this pathway is completely dependent on the SPS component, Ssy1p, and either of the transcription factors, Stp1p and Stp2p [6].

Other interactions of STP2

• In this paper, we show that Stp2p, a protein with considerable similarity to Stp1p, is also involved in the induction of BAP3 expression [7].
• Additionally, we have found that a null mutation in the ASI1 (amino acid sensor-independent) gene enables full-length unprocessed Stp1p/Stp2p to enter the nucleus and derepress SPS sensor-dependent genes [3].
• Two plasma membrane-associated proteins, Ptr3p and Ssy5p, participate in the sensing, which results in cleavage of the transcription factors Stp1p and Stp2p, removing 10 kDa of the N terminus of each of them [8].

References