Difference between revisions of "Phosphatase Subfamily PPP4C"

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(Evolution)
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_MTDP|Fold MTDP]]: [[Phosphatase_Superfamily_MTDP|Superfamily MTDP]]: [[Phosphatase_Family_PPP|Family PPP]]: [[Phosphatase_Subfamily_PPP4C|Subfamily PPP4C]]
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_MTDP|Fold MTDP]]: [[Phosphatase_Superfamily_MTDP|Superfamily MTDP]]: [[Phosphatase_Family_PPP|Family PPP]]: [[Phosphatase_Subfamily_PPP4C|Subfamily PPP4C]] (catalytic subunit of PP4 holoenzyme)
  
 
=== Evolution ===
 
=== Evolution ===
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PPP4C, catalytic subunit of Protein Phosphatase 4 (PP4) holoenzyme, is closely related to PPP2C, the catalytic subunit of PP2A holoenzyme. Like PP1 and PP2A, holoenzyme PP4 consists of the catalytic subunit and one or two regulatory subunits. At least 6 different holoenzyme complexes have been found.  
 
PPP4C, catalytic subunit of Protein Phosphatase 4 (PP4) holoenzyme, is closely related to PPP2C, the catalytic subunit of PP2A holoenzyme. Like PP1 and PP2A, holoenzyme PP4 consists of the catalytic subunit and one or two regulatory subunits. At least 6 different holoenzyme complexes have been found.  
  
Mammal PP4 participates in a number of processes essential for normal cellular physiology, including microtubule organization, homologous recombination (HR)-mediated DNA repair, the DNA damage response, histone modification, apoptosis,  immunoglobulin (Ig) VDJ recombination, pre-TCR signaling, TNF signaling, Toll-like receptor (TLR)-4 signaling, and NF-κB regulation. Germline deletion of PP4 in mice is embryonic lethal, and conditional deletion of PP4 specifically in murine T cells severely impairs T cell development. We previously ablated PP4 specifically in developing B cells using the mb-1/cre/loxP system and generated mb-1/cre/PP4F/F mice (see introduction in <cite>chen14</cite>).
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Mammal PP4 participates in a number of processes essential for normal cellular physiology, including microtubule organization, homologous recombination (HR)-mediated DNA repair, the DNA damage response, histone modification, apoptosis,  immunoglobulin (Ig) VDJ recombination, pre-TCR signaling, TNF signaling, Toll-like receptor (TLR)-4 signaling, and NF-κB regulation. Germline deletion of PP4 in mice is embryonic lethal, and conditional deletion of PP4 specifically in murine T cells severely impairs T cell development (see introduction in <cite>chen14</cite>).
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PPP4C is implicated in cancer. For instance, high expression of PPP4C is associated with the aggressive malignant behavior of colorectal carcinoma <cite>Li15</cite>.
  
 
PP4 dephoshorylate the phophorylated histone 2A variant, γ-H2AX, a marker for DNA damage and cell-cycle arrest. Interestingly, PP2A also dephosphorylates γ-H2AX.
 
PP4 dephoshorylate the phophorylated histone 2A variant, γ-H2AX, a marker for DNA damage and cell-cycle arrest. Interestingly, PP2A also dephosphorylates γ-H2AX.
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<biblio>
 
<biblio>
 
#chen14 pmid=25215539
 
#chen14 pmid=25215539
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#Li15 pmid=25927939
 
#sato14 pmid=25340746
 
#sato14 pmid=25340746
 
</biblio>
 
</biblio>

Revision as of 15:01, 1 May 2015

Phosphatase Classification: Fold MTDP: Superfamily MTDP: Family PPP: Subfamily PPP4C (catalytic subunit of PP4 holoenzyme)

Evolution

PPP4C is found in opisthokonta, amoebazoa and plants.

Domain

PPP4C has a single domain - phosphatase domain.

Functions

PPP4C, catalytic subunit of Protein Phosphatase 4 (PP4) holoenzyme, is closely related to PPP2C, the catalytic subunit of PP2A holoenzyme. Like PP1 and PP2A, holoenzyme PP4 consists of the catalytic subunit and one or two regulatory subunits. At least 6 different holoenzyme complexes have been found.

Mammal PP4 participates in a number of processes essential for normal cellular physiology, including microtubule organization, homologous recombination (HR)-mediated DNA repair, the DNA damage response, histone modification, apoptosis, immunoglobulin (Ig) VDJ recombination, pre-TCR signaling, TNF signaling, Toll-like receptor (TLR)-4 signaling, and NF-κB regulation. Germline deletion of PP4 in mice is embryonic lethal, and conditional deletion of PP4 specifically in murine T cells severely impairs T cell development (see introduction in [1]).

PPP4C is implicated in cancer. For instance, high expression of PPP4C is associated with the aggressive malignant behavior of colorectal carcinoma [2].

PP4 dephoshorylate the phophorylated histone 2A variant, γ-H2AX, a marker for DNA damage and cell-cycle arrest. Interestingly, PP2A also dephosphorylates γ-H2AX.

PP4 in C. elegans is involved in M prophase, perhaps through dephosphorylate SUN-1 protein that is normally phosphorylated during the transition zone and early pachytene [3].

References

Error fetching PMID 25215539:
Error fetching PMID 25927939:
Error fetching PMID 25340746:
  1. Error fetching PMID 25215539: [chen14]
  2. Error fetching PMID 25927939: [Li15]
  3. Error fetching PMID 25340746: [sato14]
All Medline abstracts: PubMed | HubMed