Publication Date:
2004-02-21
Description:
PTEN is a tumor suppressor protein that dephosphorylates phosphatidylinositol 3,4,5 trisphosphate and antagonizes the phosphatidylinositol-3 kinase signaling pathway. We show here that PTEN can also inhibit cell migration through its C2 domain, independent of its lipid phosphatase activity. This activity depends on the protein phosphatase activity of PTEN and on dephosphorylation at a single residue, threonine(383). The ability of PTEN to control cell migration through its C2 domain is likely to be an important feature of its tumor suppressor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftopoulou, Myrto -- Etienne-Manneville, Sandrine -- Self, Annette -- Nicholls, Sarah -- Hall, Alan -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory for Molecular Cell Biology and Cell Biology Unit, Cancer Research UK Oncogene and Signal Transduction Group, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976311" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
COS Cells
;
Catalysis
;
Catalytic Domain
;
Cell Line, Tumor
;
Cell Movement/*physiology
;
Cercopithecus aethiops
;
Glioma
;
Humans
;
Mutation
;
PTEN Phosphohydrolase
;
Phosphoprotein Phosphatases/chemistry/metabolism
;
Phosphoric Monoester Hydrolases/*chemistry/genetics/metabolism/*physiology
;
Phosphorylation
;
Phosphothreonine/metabolism
;
Precipitin Tests
;
Protein Structure, Tertiary
;
Recombinant Proteins/pharmacology
;
Sequence Deletion
;
Transfection
;
Tumor Suppressor Proteins/*chemistry/genetics/metabolism/*physiology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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