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Tytuł pozycji:

The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity.

Tytuł :
The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity.
Index Terms :
Sciences bio-médicales et agricoles
Catalysis
Electrophoresis, Polyacrylamide Gel
Glutathione Transferase -- genetics
Glutathione Transferase -- metabolism
Humans
PTEN Phosphohydrolase -- genetics
PTEN Phosphohydrolase -- metabolism
Phosphatidylinositol Phosphates -- metabolism
Phosphatidylserines -- metabolism
Phosphoric Monoester Hydrolases -- genetics
Phosphoric Monoester Hydrolases -- metabolism
Phosphorylation
Recombinant Fusion Proteins -- genetics
Recombinant Fusion Proteins -- metabolism
Substrate Specificity
Transport Vesicles -- metabolism
Inositol 5-phosphatase
Lipid
Phosphatidylserine
Phosphoinositide
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
Wydawca :
2006-12
Dodane szczegóły :
Vandeput, Fabrice
Backers, Katrien
Villeret, Vincent
Pesesse, Xavier
Erneux, Christophe
Typ dokumentu :
Zasób elektroniczny
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52140">http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52140
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL">http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Dostępność :
Open access content. Open access content
1 full-text file(s): info:eu-repo/semantics/restrictedAccess
Pozostałe numery :
EQY oai:dipot.ulb.ac.be:2013/52140
uri/info:doi/10.1016/j.cellsig.2006.05.010
uri/info:pii/S0898-6568(06)00104-5
uri/info:pmid/16824732
uri/info:scp/33750336748
https://dipot.ulb.ac.be/dspace/bitstream/2013/52140/1/Elsevier_27308.pdf
764632616
Źródło wspomagające :
UNIV LIBR DE BRUXELLES
From OAIster®, provided by the OCLC Cooperative.
Numer akcesji :
edsoai.ocn764632616
Zasób elektroniczny
The SH2 domain containing inositol 5-phosphatase 2 (SHIP2) catalyzes the dephosphorylation of phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P(2)) and participates in the insulin signalling pathway in vivo. In a comparative study of SHIP2 and the phosphatase and tensin homologue deleted on chromosome 10 (PTEN), we found that their lipid phosphatase activity was influenced by the presence of vesicles of phosphatidylserine (PtdSer). SHIP2 PtdIns(3,4,5)P(3) 5-phosphatase activity was greatly stimulated in the presence of vesicles of PtdSer. This effect appears to be specific for di-C8 and di-C16 fatty acids of PtdIns(3,4,5)P(3) as substrate. It was not observed with inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P(4)) another in vitro substrate of SHIP2, nor with Type I Ins(1,4,5)P(3)/Ins(1,3,4,5)P(4) 5-phosphatase activity, an enzyme which acts on soluble inositol phosphates. Vesicles of phosphatidylcholine (PtdCho) stimulated only twofold PtdIns(3,4,5)P(3) 5-phosphatase activity of SHIP2. Both a minimal catalytic construct and the full length SHIP2 were sensitive to the stimulation by PtdSer. In contrast, PtdIns(3,4,5)P(3) 5-phosphatase activity of the Skeletal muscle and Kidney enriched Inositol Phosphatase (SKIP), another member of the mammaliam Type II phosphoinositide 5-phosphatases, was not sensitive to PtdSer. Our enzymatic data establish a specificity in the control of SHIP2 lipid phosphatase activity with PtdIns(3,4,5)P(3) as substrate which is depending on the fatty acid composition of the substrate.
Journal Article
Research Support, Non-U.S. Gov't
info:eu-repo/semantics/published

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