keyword
MENU ▼
Read by QxMD icon Read
search

Syk 342

keyword
https://www.readbyqxmd.com/read/20828828/syk-and-lyn-mediate-distinct-syk-phosphorylation-events-in-fc%C3%A9-ri-signal-transduction-implications-for-regulation-of-ige-mediated-degranulation
#1
Michael P Sanderson, Eva Wex, Takeshi Kono, Katsuhiro Uto, Andreas Schnapp
Spleen tyrosine kinase (Syk) is a key regulatory factor in the IgE-mediated allergic signal transduction pathway in mast cells and basophils. Syk is phosphorylated on a number of tyrosines following the binding of IgE/allergen complexes to FcɛRI receptors leading to initiation of inflammatory signaling via downstream enzymes and scaffolding proteins. We examined the kinases responsible for the phosphorylation of key Syk tyrosines in rat RBL-2H3 basophilic cells and bone marrow-derived mast cells (BMMCs). The phosphorylation of Syk tyrosine 346 was completely blocked by the novel Src family kinase inhibitor BIRA766, suggesting this tyrosine is a pure substrate for Src family kinases...
November 2010: Molecular Immunology
https://www.readbyqxmd.com/read/19435818/role-of-the-protein-tyrosine-kinase-syk-in-regulating-cell-cell-adhesion-and-motility-in-breast-cancer-cells
#2
Xiaoying Zhang, Ulka Shrikhande, Bethany M Alicie, Qing Zhou, Robert L Geahlen
The expression of the Syk protein tyrosine kinase in breast cancer cells is inversely correlated with invasive growth and metastasis. The expression of Syk inhibits cell motility while supporting the formation of cell clusters by enhancing cell-cell contacts and promoting the redistribution of the adhesion proteins cortactin and vinculin to these contacts. Syk associates physically with cortactin and catalyzes its phosphorylation on tyrosine. The clustering of integrins leads to the phosphorylation of Syk and of numerous cellular proteins in a manner dependent on the activity of the kinase and on the presence of tyrosine 342 located in the linker B region...
May 2009: Molecular Cancer Research: MCR
https://www.readbyqxmd.com/read/12077122/regulation-of-signaling-in-b-cells-through-the-phosphorylation-of-syk-on-linker-region-tyrosines-a-mechanism-for-negative-signaling-by-the-lyn-tyrosine-kinase
#3
Julie J Hong, Thomas M Yankee, Marietta L Harrison, Robert L Geahlen
The B cell antigen receptor (BCR) is coupled to the mobilization of Ca(2+) by the protein-tyrosine kinase, Syk. Syk, recruited to the clustered BCR, becomes phosphorylated on three tyrosines (Tyr-317, Tyr-342, and Tyr-346) located within the linker region that separates the C-terminal catalytic domain from the N-terminal tandem Src homology 2 domains. Phosphorylation within the linker region can be either activating or inhibitory to Ca(2+) mobilization depending on the sites that are modified. Syk that is not phosphorylated on linker region tyrosines couples the BCR to Ca(2+) mobilization through a phosphoinositide 3-kinase-dependent pathway...
August 30, 2002: Journal of Biological Chemistry
1
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"