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 SOX9
Homo sapiens
 HIF1A
Homo sapiens
 Pax6
Mus musculus
 PAX6
Homo sapiens
 Snai2
Mus musculus
 PPARA
Homo sapiens
 Ppara
Mus musculus
 Thrb
Mus musculus
 SNAI2
Homo sapiens
 Tbr1
Mus musculus
Transcription Factor Encyclopedia  BETA
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Isoforms
No annotation is available in this section for this article. The content below is taken from a related TF, ZBTB16 (Homo sapiens).

The human PLZF gene contains six exons and five introns, and there are at least four alternative splice isoforms within a large exon 1. There are no reports of functional splice isoforms for PLZF. However, a hepatocytic isoform has been identified that lacks its BTB domain and its expression was confirmed by Western blot in HepG2 hepatocarcinoma cells. It remains unclear as to whether this 45-kDa PLZF protein can be translated from another variant of the alternatively spliced PLZF, or if other modifying mechanisms are employed. Also, while this isoform localized to the trans-Golgi complexes of HepG2 cells, its function remains unclear.

In cases of acute promyelocytic leukaemia (APL), as a result of a t(11;17) reciprocal chromosomal translocation, mRNAs containing the coding sequences of PLZF are fused in-frame either upstream of the RAR alpha B region or downstream from the unique A1 and A2 regions of the two major RAR alpha isoforms. These are expressed from the rearranged alleles and expression of these fusions affects the expression of RAR alpha target genes involved in DNA repair, apoptosis and cell cycle because of the inappropriate recruitment of nuclear corepressor molecules.

Covalent modifications
No annotation is available in this section for this article. The content below is taken from a related TF, ZBTB16 (Homo sapiens).

PLZF is subject to several different post-translational modifications, including, phosphorylation, acetylation and conjugation to ubiquitin and SUMO-1.

PLZF is acetylated by the histone acetyltransferase (HAT) p300, where acetylation of lysines in its C-terminal C2H2 zinc finger motif is required for its ability to repress transcription. Acetylation of PLZF also activates its ability to bind specific DNA sequences both in vitro and in vivo. An acetylation site mutant of PLZF does not repress transcription despite maintaining an interaction with corepressor/histone deacetylase complexes. The cyclin-dependent kinase CDK2 phosphorylates PLZF at two consensus sites found within PEST domains present in the hinge region of the protein. This phosphorylation triggers the ubiquitination and subsequent degradation of PLZF. Also, in natural killer cells, interferon-induced phosphorylation of PLZF within its BTB domain by JNK kinase cascades has been suggested to trigger a repressor-to-activator switch, where PLZF binds to HDAC1 in a manner that is dependent on the phosphorylation.

PLZF is modified by SUMO-1 at lysine 242 in the RD2 domain and this modification is required for transcriptional repression by PLZF. Electrophoretic mobility shift assay showed that this SUMO-modification increases the DNA binding activity of PLZF. This lysine residue can also be ubiquinated, where stability and nuclear localization of PLZF were regulated by the antagonistic relationship between sumoylation and ubiquitination.