Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person Signaling via FGFRs is mediated via direct recruitment of si...

Class:IdSummation:191012
_displayNameSignaling via FGFRs is mediated via direct recruitment of si...
_timestamp2011-07-06 20:46:56
created[InstanceEdit:191011] de Bono, B, 2007-01-11 13:37:10
literatureReference[LiteratureReference:190609] Cellular signaling by fibroblast growth factor receptors
[LiteratureReference:190605] Mechanisms underlying differential responses to FGF signaling
[LiteratureReference:191518] Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
[LiteratureReference:1295595] Comparison of the intracellular signaling responses by three chimeric fibroblast growth factor receptors in PC12 cells
modified[InstanceEdit:191530] de Bono, B, 2007-01-20 15:27:43
[InstanceEdit:1268195] Rothfels, K, 2011-05-09
[InstanceEdit:1295635] Rothfels, K, 2011-05-17
[InstanceEdit:1384569] Rothfels, K, 2011-07-06
textSignaling via FGFRs is mediated via direct recruitment of signaling proteins that bind to tyrosine auto-phosphorylation sites on the activated receptor and via closely linked docking proteins that become tyrosine phosphorylated in response to FGF-stimulation and form a complex with additional complement of signaling proteins.

The activation loop in the catalytic domain of FGFR maintains the PTK domain in an inactive or low activity state. The activation-loop of FGFR1, for instance, contains two tyrosine residues that must be autophosphorylated for maintaining the catalytic domain in an active state. In the autoinhibited configuration, a kinase invariant proline residue at the C-terminal end of the activation loop interferes with substrate binding while allowing access to ATP in the nucleotide binding site.
In addition to the catalytic PTK core, the cytoplasmic domain of FGFR contains several regulatory sequences. The juxtamembrane domain of FGFRs is considerably longer than that of other receptor tyrosine kinases. This region contains a highly conserved sequence that serves as a binding site for the phosphotyrosine binding (PTB) domain of FRS2. A variety of signaling proteins are phosphorylated in response to FGF stimulation, including Shc, phospholipase-C gamma and FRS2 leading to stimulation of intracellular signaling pathways that control cell proliferation, cell differentiation, cell migration, cell survival and cell shape.
(summation)[Pathway:5654687] Downstream signaling of activated FGFR1 [Homo sapiens]
[Pathway:5654696] Downstream signaling of activated FGFR2 [Homo sapiens]
[Pathway:5654708] Downstream signaling of activated FGFR3 [Homo sapiens]
[Pathway:5654716] Downstream signaling of activated FGFR4 [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Signaling via FGFRs is mediated via direct recruitment of si... (191012)