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• W1798533689 abstract "Abstract Phosphoinositide (PI) phosphatases such as the SH2 domain‐containing inositol 5‐phosphatases 1/2 (SHIP1 and 2) are important signalling enzymes in human physiopathology. SHIP1/2 interact with a large number of immune and growth factor receptors. Tyrosine phosphorylation of SHIP1/2 has been considered to be the determining regulatory modification. However, here we present a hypothesis, based on recent key publications, highlighting the determining role of Ser/Thr phosphorylation in regulating several key properties of SHIP1/2. Since a subunit of the Ser/Thr phosphatase PP2A has been shown to interact with SHIP2, a putative mechanism for reversing SHIP2 Ser/Thr phosphorylation can be anticipated. PI phosphatases are potential target molecules in human diseases, particularly, but not exclusively, in cancer and diabetes. Therefore, this novel regulatory mechanism deserves further attention in the hunt for discovering novel or complementary therapeutic strategies. This mechanism may be more broadly involved in regulating PI signalling in the case of synaptojanin1 or the phosphatase, tensin homolog, deleted on chromosome TEN. Editor's suggested further reading in BioEssays: Pairing phosphoinositides with calcium ions in endolysosomal dynamics Abstract" @default.
• W1798533689 created "2016-06-24" @default.
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• W1798533689 date "2012-05-29" @default.
• W1798533689 modified "2023-10-17" @default.
• W1798533689 title "Reversible Ser/Thr SHIP phosphorylation: A new paradigm in phosphoinositide signalling?" @default.
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• W1798533689 doi "https://doi.org/10.1002/bies.201100195" @default.
• W1798533689 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22641604" @default.
• W1798533689 hasPublicationYear "2012" @default.
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