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Src (36D10) Rabbit mAb antibody

RRID:AB_10693939

Antibody ID

AB_2106059

Target Antigen

Src (36D10) Rabbit mAb porcine, bovine, hamster, mouse, human, non-human primate, rat, h, m, r, hm, mk, b, pg

Vendor

Cell Signaling Technology

Cat Num

2109

Proper Citation

(Cell Signaling Technology Cat# 2109, RRID:AB_2106059)

Clonality

monoclonal antibody

Host Organism

rabbit

Comments

Applications: W, IP, IHC-P, IF-F, IF-IC, F. Consolidation on 10/2018: AB_10693939, AB_2106059. Info: Used By NYUIHC-1403.

Publications that use this research resource

Lck/Hck/Fgr-Mediated Tyrosine Phosphorylation Negatively Regulates TBK1 to Restrain Innate Antiviral Responses.

  • Liu S
  • Cell Host Microbe
  • 2017 Jun 14

Literature context: at#2109S; RRID:AB_10693939 Rabbit mon


Abstract:

Cytosolic nucleic acid sensing elicits interferon production for primary antiviral defense through cascades controlled by protein ubiquitination and Ser/Thr phosphorylation. Here we show that TBK1, a core kinase of antiviral pathways, is inhibited by tyrosine phosphorylation. The Src family kinases (SFKs) Lck, Hck, and Fgr directly phosphorylate TBK1 at Tyr354/394, to prevent TBK1 dimerization and activation. Accordingly, antiviral sensing and resistance were substantially enhanced in Lck/Hck/Fgr triple knockout cells and ectopic expression of Lck/Hck/Fgr dampened the antiviral defense in cells and zebrafish. Small-molecule inhibitors of SFKs, which are conventional anti-tumor therapeutics, enhanced antiviral responses and protected zebrafish and mice from viral attack. Viral infection induced the expression of Lck/Hck/Fgr through TBK1-mediated mobilization of IRF3, thus constituting a negative feedback loop. These findings unveil the negative regulation of TBK1 via tyrosine phosphorylation and the functional integration of SFKs into innate antiviral immunity.

Ambra1 spatially regulates Src activity and Src/FAK-mediated cancer cell invasion via trafficking networks.

  • Schoenherr C
  • Elife
  • 2017 Mar 31

Literature context: e 36D10) (RRID:AB_10693939), anti-LC3


Abstract:

Here, using mouse squamous cell carcinoma cells, we report a completely new function for the autophagy protein Ambra1 as the first described 'spatial rheostat' controlling the Src/FAK pathway. Ambra1 regulates the targeting of active phospho-Src away from focal adhesions into autophagic structures that cancer cells use to survive adhesion stress. Ambra1 binds to both FAK and Src in cancer cells. When FAK is present, Ambra1 is recruited to focal adhesions, promoting FAK-regulated cancer cell direction-sensing and invasion. However, when Ambra1 cannot bind to FAK, abnormally high levels of phospho-Src and phospho-FAK accumulate at focal adhesions, positively regulating adhesion and invasive migration. Spatial control of active Src requires the trafficking proteins Dynactin one and IFITM3, which we identified as Ambra1 binding partners by interaction proteomics. We conclude that Ambra1 is a core component of an intracellular trafficking network linked to tight spatial control of active Src and FAK levels, and so crucially regulates their cancer-associated biological outputs.

Funding information:
  • European Research Council - 294440()