Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 proce... more Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 processing, suggesting The OLE pathway of yeast regulates the level of the ER-
The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase ... more The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase OLE1, thereby controlling membrane fluidity. A central component of this regulon is the transcription factor SPT23, a homolog of mammalian NF-kappaB. SPT23 is synthesized as an inactive, ER membrane-anchored precursor that is activated by regulated ubiquitin/proteasome-dependent processing (RUP). We now show that SPT23 dimerizes prior to processing and that the processed molecule, p90, retains its ubiquitin modification and initially remains tethered to its unprocessed, membrane-bound SPT23 partner. Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex. Remarkably, this enzyme binds preferentially ubiquitinated substrates, suggesting that CDC48(UFD1/NPL4) is qualified to selectively remove ubiquitin conjugates from protein complexes.
Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 proce... more Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 processing, suggesting The OLE pathway of yeast regulates the level of the ER-
Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 proce... more Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 processing, suggesting The OLE pathway of yeast regulates the level of the ER-
The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase ... more The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase OLE1, thereby controlling membrane fluidity. A central component of this regulon is the transcription factor SPT23, a homolog of mammalian NF-kappaB. SPT23 is synthesized as an inactive, ER membrane-anchored precursor that is activated by regulated ubiquitin/proteasome-dependent processing (RUP). We now show that SPT23 dimerizes prior to processing and that the processed molecule, p90, retains its ubiquitin modification and initially remains tethered to its unprocessed, membrane-bound SPT23 partner. Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex. Remarkably, this enzyme binds preferentially ubiquitinated substrates, suggesting that CDC48(UFD1/NPL4) is qualified to selectively remove ubiquitin conjugates from protein complexes.
Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 proce... more Summary the nucleus to drive OLE1 transcription. High levels of UFAs completely block SPT23 processing, suggesting The OLE pathway of yeast regulates the level of the ER-
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Papers by Marian Kalocay