Difference between revisions of "Phosphatase Family LMWPTP"
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Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo <cite>Magherini</cite>, on a residue likely phosphorylated by CK2 <cite>Wilson</cite>. | Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo <cite>Magherini</cite>, on a residue likely phosphorylated by CK2 <cite>Wilson</cite>. | ||
| − | In prokaryotes, the molecular function is not fully understood. It is involved in the syntheisis and translocation of exopolysaccharides (EPS) and capsular polysaccharides (CPS) in E. coli. YwlE also acts as an arginine phosphatase <cite>Fuhrmann</cite> | + | In prokaryotes, the molecular function is not fully understood. It is involved in the syntheisis and translocation of exopolysaccharides (EPS) and capsular polysaccharides (CPS) in E. coli. YwlE also acts as an arginine phosphatase <cite>Fuhrmann</cite>. In many species, the LMWPTP is chromosomally adjacent to a fructosamine kinase, suggesting that it's major role is in protein deglycation <cite>Gemayel</cite>. E. coli Wzb is known to dephosphorylate the atypical tyrosine kinase Wzc <cite>Temel</cite>. |
== Reference == | == Reference == | ||
<biblio> | <biblio> | ||
| + | #Temel pmid=23543749 | ||
| + | #Gemayel pmid=17681011 | ||
#Van pmid=20967558 | #Van pmid=20967558 | ||
#Alho pmid=23584899 | #Alho pmid=23584899 | ||
Revision as of 04:16, 1 May 2014
Phosphatase Classification: Superfamily Cys-based III: Family LMWPTP
Evolution
The LMWPTP is present not only in eukaryotes but also prokaryotes. In eukaryotes, it is generally absent from alveolates, trypanosoma, leishmania.
Domain Structure
Most LMWPTP consist almost entirely of a phosphatase domain
Function
In eukaryotes, LMWPTP dephosphorylates many receptor tyrosine kinases, such PDGFR, InsR, and Eph [1]. It is a substrate for Src and Src phosphorylation creates a Grb2 SH2 domain-binding site. Accordingly it has been implicated in cancer progression [2]. Polymorphisms have also been implicated in metabolic and immune diseases.
Human LMWPTP is also known to be a declycating agent, removing ribulose 5-phosphate from proteins [3, 4], in collaboration with Fructosamine Kinase.
Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo [5], on a residue likely phosphorylated by CK2 [6].
In prokaryotes, the molecular function is not fully understood. It is involved in the syntheisis and translocation of exopolysaccharides (EPS) and capsular polysaccharides (CPS) in E. coli. YwlE also acts as an arginine phosphatase [7]. In many species, the LMWPTP is chromosomally adjacent to a fructosamine kinase, suggesting that it's major role is in protein deglycation [8]. E. coli Wzb is known to dephosphorylate the atypical tyrosine kinase Wzc [9].
Reference
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