Difference between revisions of "Phosphatase Subfamily PTEN"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTEN|Family PTEN]]: [[Phosphatase_Subfamily_PTEN|Subfamily PTEN]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTEN|Family PTEN]]: [[Phosphatase_Subfamily_PTEN|Subfamily PTEN]] | ||
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PTEN subfamily is named after its single member in human, PTEN, which dephosphorylates phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)P3 or PIP3). PTEN is one of the most commonly lost tumor suppressors in human cancer. | PTEN subfamily is named after its single member in human, PTEN, which dephosphorylates phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)P3 or PIP3). PTEN is one of the most commonly lost tumor suppressors in human cancer. | ||
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===Domain Structure=== | ===Domain Structure=== | ||
Most PTEN have a phosphatase domain followed by a C2 domain. Some homologs have PH (phospholipid-binding) or LIM domains, but these are not conserved. | Most PTEN have a phosphatase domain followed by a C2 domain. Some homologs have PH (phospholipid-binding) or LIM domains, but these are not conserved. | ||
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| + | C2 domain tethers PTEN to vesicles by specifically binding to phosphatidylinositol 3-phosphate (PI(3)P) (the signature lipid of endosomes) through the CBR3 loop (see [http://www.cell.com/molecular-cell/abstract/S1097-2765(15)00176-8?rss=yes here]). | ||
===Functions=== | ===Functions=== | ||
| − | PTEN is a critical negative regulator of PI3K signaling. | + | PTEN is a critical negative regulator of PI3K signaling. PI3K produce the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PI (3,4,5)) trisphosphate (PI(3,4,5)P3/PIP3) in response to activation of receptor tyrosine kinases (RTKs), G-protein-coupled receptors, or membrane-bound oncogenes <cite>Engelman06, Vanhaesebroeck12</cite>. It dephosphorylates the lipid second messenger, PI (3,4,5) <cite>Maehama98</cite>. It is tumor suppressor among the most frequently altered genes in cancer <cite>Li97, Steck97</cite>. |
===References=== | ===References=== | ||
<biblio> | <biblio> | ||
| + | #Engelman06 pmid=16847462 | ||
| + | #Li97 pmid=9072974 | ||
| + | #Maehama98 pmid=9593664 | ||
| + | #Steck97 pmid=9090379 | ||
| + | #Vanhaesebroeck12 pmid=22358332 | ||
</biblio> | </biblio> | ||
Revision as of 19:41, 9 April 2015
Phosphatase Classification: Superfamily CC1: Family PTEN: Subfamily PTEN
PTEN subfamily is named after its single member in human, PTEN, which dephosphorylates phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)P3 or PIP3). PTEN is one of the most commonly lost tumor suppressors in human cancer.
Evolution
PTEN is found in almost all eukaryotes.
Domain Structure
Most PTEN have a phosphatase domain followed by a C2 domain. Some homologs have PH (phospholipid-binding) or LIM domains, but these are not conserved.
C2 domain tethers PTEN to vesicles by specifically binding to phosphatidylinositol 3-phosphate (PI(3)P) (the signature lipid of endosomes) through the CBR3 loop (see here).
Functions
PTEN is a critical negative regulator of PI3K signaling. PI3K produce the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PI (3,4,5)) trisphosphate (PI(3,4,5)P3/PIP3) in response to activation of receptor tyrosine kinases (RTKs), G-protein-coupled receptors, or membrane-bound oncogenes [1, 2]. It dephosphorylates the lipid second messenger, PI (3,4,5) [3]. It is tumor suppressor among the most frequently altered genes in cancer [4, 5].
References
Error fetching PMID 9072974:
Error fetching PMID 9593664:
Error fetching PMID 9090379:
Error fetching PMID 22358332:
- Error fetching PMID 16847462:
- Error fetching PMID 22358332:
- Error fetching PMID 9593664:
- Error fetching PMID 9072974:
- Error fetching PMID 9090379:
