A dangerous gene PTPRT (PTPrho)

 If you follow our blogs, you will be aware of 3 things about why a gene could be dangerous,
1. Its ability to induce malformation once absent
2. Its interaction with either multiple other genes but particularly its involvement with a "wild gene", genes that are cofactors to anything happening in the cell (Gerb2,FYN) or globally a gene that have just too many interactions with other genes (Androgen related gene).
3.In terms of cancer metastasis and non-curability, the gene involvement with the Wnt (cathenin) and the Notch.  Involvement with the Rho increases the rate of multiplication. 

Based on these criteria, PTPRT (PTPrho) wins the cake!
It is stimulated by Actinin alpha 1
which itself interacts with:


Actinin, alpha 1 has been shown to interact with:

• CDK5R1,^[3]
• CDK5R2,^[3]
• Collagen, type XVII, alpha 1,^[4]
• GIPC1,^[5]
• PDLIM1,^[6][7]
• Protein kinase N1,^[8]
• SSX2IP,^[9] and
• Zyxin.^[10][11]
• PTPRT(PTPrho)^{[12] wikipedia}
• 
  
• ^{The involvement with GIPC1 needs to be noted! because it provide the link to DAB2, a gene suppressed in Ovarian cancers!  GIPC1 reaches DAB2 through MYO-6.}
• 
  
• ^{well Actinin}

 ===================================================FROM WIKIPEDIA, THIS FOLLOW:"
Receptor-type tyrosine-protein phosphatase T is an enzyme that in humans is encoded by the PTPRT gene.^[1][2][3]
PTPRT is also known as PTPrho, PTPρ and human accelerated region 9. The human accelerated regions are 49 regions of the human genome that are conserved among vertebrates, but in humans show significant distinction from other vertebrates. This region may, therefore, have played a key role in differentiating humans from apes.^[4]
PTPrho is phosphorylated on tyrosine 912 in the wedge region of its first catalytic domain by Fyn tyrosine kinase. Phosphorylation at this site attenuates synapse formation in cultured neurons. When PTPrho is phosphorylated by Fyn, PTPrho appears to form homophilic multimerizations, likely in cis, which appear to decrease PTPrho association with neuroligins and neurexins. The reduction of cis interactions with neuroligins and neurexons is hypothesized to ultimately lead to the reduction in synapse formation.^[12]



Evaluation of the 5’untranslated regions of PTPrho (PTPRT) cDNA indicate a number of transcription factor binding site consensus sequences, including those for AP-2, c-Myb, NF-1, sox-5, and Sp-1, Oct-1, CdxA, C/EBP, En-1, GATA-1, GATA-2, GKLF, HoxA3, Ik-2, Msx-1, Pax-4 and SRY.^[5]
(RE1-silencing transcription factor) (REST) is a transcription repressor that binds to REST DNA recognition element (RE-1) in 5’UTRs. A screen of single nucleotide polymorphic genetic changes within the REST binding regions of DNA sequences revealed a polymorphism in the RE-1 of PTPrho (PTPRT). This SNP would result in less REST repressor activity, which could lead to increased expression of PTPrho (PTPRT) in cells that harbored this SNP.^[15]
 PTPrho is also upregulated in estrogen receptor alpha positive breast tumor samples versus estrogen receptor alpha negative tumor samples.^[18] The authors evaluated 560 selected genes by real-time quantitative reverse transcription-polymerase chain reaction (RT-PCR) in estrogen receptor alpha positive tissue and compared it to estrogen receptor alpha negative tissue, and found that PTPrho(PTPRT) was upregulated in the estrogen receptor alpha tissue, suggesting a non-tumor suppressor role for PTPrho. ^[18]"