Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kuehbacher, A.; Dambournet, D.; Echard, A.; Cossart, P.; Pizarro-Cerda, J.
    Phosphatidylinositol 5-phosphatase oculocerebrorenal syndrome of Lowe protein (OCRL) controls actin dynamics during early steps of Listeria monocytogenes infection (2012), J. Biol. Chem., 287, 13128-13136.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.36 Listeria monocytogenes
-
-
-
3.1.3.86 Danio rerio
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.86 neutrophil
-
Danio rerio
-

Synonyms

EC Number Synonyms Comment Organism
3.1.3.36 OCRL
-
Listeria monocytogenes
3.1.3.86 SH2-domain-containing 5-inositol phosphatase
-
Danio rerio
3.1.3.86 SHIP
-
Danio rerio

General Information

EC Number General Information Comment Organism
3.1.3.36 malfunction in cells knocked down for OCRL, transfection of enzymatically active EGFP-OCRL-a (but not of a phosphatase-dead enzyme) decreases the levels of intracellular Listeria monocytogenes and of actin associated with invading bacteria Listeria monocytogenes
3.1.3.36 malfunction inactivation of OCRL by siRNA leads to an increase in the internalization levels of Listeria monocytogenes in HeLa cells. OCRL depletion does not increase but rather decreases the surface expression of the receptor Met Listeria monocytogenes
3.1.3.36 physiological function by reducing the levels of PI(4,5)P2 and PI(3,4,5)P3 at the plasma membrane, OCRL restricts infection through modulation of actin dynamics at bacterial internalization sites Listeria monocytogenes
3.1.3.86 malfunction depletion of SHIP 5'-phosphatases increases neutrophil wound attraction and random motility through a PI3K-dependent pathway. Ectopic expression of the SHIP1 phosphatase domain impairs neutrophil migration Danio rerio
3.1.3.86 physiological function SHIP phosphatases serve as a brake that limit neutrophil motility and inflammation, at least in part through their effects on PI3K signaling Danio rerio