2016 Group Project 3: Difference between revisions
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22 protein families of have been identified from the FGF signalling pathway, 18 of which are secreted signalling proteins (FGF1-10, and FGF16-23) that interact with 4 tyrosine kinase FGF Receptors (FGFR1-4) and the other 4 are intracellular non-signalling proteins (iFGFs; FGF11-14). | 22 protein families of have been identified from the FGF signalling pathway, 18 of which are secreted signalling proteins (FGF1-10, and FGF16-23) that interact with 4 tyrosine kinase FGF Receptors (FGFR1-4) and the other 4 are intracellular non-signalling proteins (iFGFs; FGF11-14). | ||
<ref><pubmed>25772309</pubmed>[http://www.ncbi.nlm.nih.gov/pubmed/25772309]</ref> | <ref><pubmed>25772309</pubmed>[http://www.ncbi.nlm.nih.gov/pubmed/25772309]</ref> | ||
FGFRs are comprised of 3 immunoglobulin domains (IgI-III), with IgIII being the closest to the transmembrane, and IgI being the furthest away. As shown in the image, an acidic box (AD) is located in-between IgI and IgII, IgII contains a heparin-binding domain (HBD), which is important in signal transduction, and IgIII is a transmembrane structure with kinase and interkinase domains (KD and IKD) within the intracellular space. <ref><pubmed>16216232</pubmed>[http://www.ncbi.nlm.nih.gov/pubmed/16216232]</ref> | |||
===Signal Transduction=== | ===Signal Transduction=== | ||
FGF ligands linked to heparin sulfate proteoglycan (HSPG) bind to both the IgII and IgIII domain of the receptor (with the heparin component specifically binding to IgII) resulting in dimerisation of the receptors and activation of signal transduction pathways through the phosphorylation of tyrosine residues. | |||
(Still finishing will add in an image too) | (Still finishing will add in an image too) |
Revision as of 10:24, 15 September 2016
2016 Student Projects | ||||
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Signalling: 1 Wnt | 2 Notch | 3 FGF Receptor | 4 Hedgehog | 5 T-box | 6 TGF-Beta | ||||
2016 Group Project Topic - Signaling in Development
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This page is an undergraduate science embryology student project and may contain inaccuracies in either descriptions or acknowledgements. |
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Fibroblast Growth Factor Receptor (FGFR) Pathway
Introduction
The Fibroblast Growth Factor (FGF) signalling pathway is critical for regulating progenitor cell proliferation, differentiation, survival and patterning. It is involved in the regulation and development of the early embryo, and is considered to be critical for normal organ, vascular and skeletal development. Furthermore, this pathway is also involved in maintaining adult tissues through the regulation of metabolic functions and tissue repair (which is often through the reactivation of the same signalling pathways involved in early development.) [1]
History
Fibroblast growth factor (FGF) was initially discovered in pituitary extracts through experiments conducted in 1973. Researchers had noticed the growth stimulating effects that these isolated factors had, in that they induced fibroblast proliferation. Due to their ability to stimulate fibroblast proliferation they were termed "FGFs". Today, a variety of subtypes of FGFs have been discovered and categorised into a large family that exist in organisms including humans as well as nematodes. In addition, it was soon discovered that not all FGFs can stimulate fibroblasts.
Overview Of The FGFR Pathway
22 protein families of have been identified from the FGF signalling pathway, 18 of which are secreted signalling proteins (FGF1-10, and FGF16-23) that interact with 4 tyrosine kinase FGF Receptors (FGFR1-4) and the other 4 are intracellular non-signalling proteins (iFGFs; FGF11-14). [2]
FGFRs are comprised of 3 immunoglobulin domains (IgI-III), with IgIII being the closest to the transmembrane, and IgI being the furthest away. As shown in the image, an acidic box (AD) is located in-between IgI and IgII, IgII contains a heparin-binding domain (HBD), which is important in signal transduction, and IgIII is a transmembrane structure with kinase and interkinase domains (KD and IKD) within the intracellular space. [3]
Signal Transduction
FGF ligands linked to heparin sulfate proteoglycan (HSPG) bind to both the IgII and IgIII domain of the receptor (with the heparin component specifically binding to IgII) resulting in dimerisation of the receptors and activation of signal transduction pathways through the phosphorylation of tyrosine residues.
(Still finishing will add in an image too)
Role In Embryonic Development
Patterning Of The Embryonic Axis
Induction/Maintenance Of Mesoderm And Neuroectoderm
Organogenesis
Limb Bud
(Kristine)
Kidney/External Genitalia
Animal Models
Abnormalities
(Kristine)
References
Extra Resources
Useful review articles that may be worth a read through:
http://onlinelibrary.wiley.com/doi/10.1002/wdev.176/full
http://www.nature.com.wwwproxy0.library.unsw.edu.au/nrd/journal/v8/n3/pdf/nrd2792.pdf
http://www.sciencedirect.com.wwwproxy0.library.unsw.edu.au/science/article/pii/S0012160605006184
http://www.nature.com.wwwproxy0.library.unsw.edu.au/nrm/journal/v14/n3/full/nrm3528.html
http://onlinelibrary.wiley.com.wwwproxy0.library.unsw.edu.au/doi/10.1002/jcp.24649/full
http://genesdev.cshlp.org/content/29/14/1463.full (FGF signalling and skeletogenesis, specifically how mutations to the FGF signalling pathway may be responsible for skeletal diseases)