Gene interactions and pathways from curated databases and text-mining

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SRC — SYK

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Pisegna et al., J Immunol 2002 : Src dependent Syk activation controls CD69 mediated signaling and function on human NK cells
Melander et al., Biochem J 2003 : The following observations imply that Syk is such a kinase : ( i ) beta ( 2 ) integrins activated Syk in a Src dependent manner, ( ii ) Syk was associated with Cbl much longer than Fgr was, and ( iii ) the Syk inhibitor piceatannol ( 3,4,3',5'-tetrahydroxy- trans -stilbene ) abolished the Cbl associated kinase activity in an in vitro assay
Dangelmaier et al., Blood 2005 : The Src family kinase inhibitors prevented Syk phosphorylation and its ubiquitination, indicating that the process is downstream of Src kinases
Leoncini et al., J Cell Biochem 2007 : Likely oxidative stress could prime the non receptor mediated tyrosine kinase p60src , inducing phosphorylation and activation of p72syk
Lee et al., Arch Pharm Res 2007 : In this study, we focused on investigating the roles of Syk in the regulation of Src signaling in PDGF mediated vascular cell responses
Kahner et al., Platelets 2008 : Further Syk activation, as measured by tyrosine phosphorylation of Syk ( residues 525/526 ), in response to PAR activation was abolished in the presence of Src inhibitors
Kato et al., Platelets 2009 : In vitro kinase assay with GST-Syk and -Aup1 proteins at the presence or absence of active Src, a potent activator of Syk, revealed that Aup1 does not directly influence activation of Syk by autophosphorylation or tyrosine phosphorylation by Src
Chang et al., PloS one 2012 (MAP Kinase Signaling System) : PKC can activate LKB1/AMPK, leading to phosphorylation and activation of Syk , and subsequent activation of Src and FAK
Takata et al., FEBS Lett 1995 : Kinase activity of Src-PTK was essential for tyrosine phosphorylation of Syk and calcium mobilization upon receptor ligation, whereas these events were not affected by the mutation of SH2 domain