Sandbox Reserved 1124: Difference between revisions
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== Disease == | == Disease == | ||
Grb2 is an intermediate protein and recruits signalling molecules to form complexes. These signalling complexes cause cellular responses like cellular proliferation or invasion which can have an impact in cancer. Grb2 can also occur in many other stages of the cancer progression : it can lead to tumorigenesis.<ref>DOI:10.1517/14728222.12.8.1021</ref> Moreover, the phosphorylation of the 160 tyrosine on Grb2 has been observed in many human cancers such as prostate, colon or breast cancers and the switch between the dimeric and monomeric conformations regulates the cancer progression. | Grb2 is an intermediate protein and recruits signalling molecules to form complexes. These signalling complexes cause cellular responses like cellular proliferation or invasion which can have an impact in cancer. Grb2 can also occur in many other stages of the cancer progression : it can lead to tumorigenesis.<ref>DOI:10.1517/14728222.12.8.1021</ref> Moreover, the phosphorylation of the 160 tyrosine on Grb2 has been observed in many human cancers such as prostate, colon or breast cancers and the switch between the dimeric and monomeric conformations regulates the cancer progression.<ref >PMID: 26234419</ref> | ||
Several mutations in the SH2 domain can cause human diseases such as Noonan syndrome or basal cell carcinoma. For example, it can have a suppression of phosphotyrosine dependent interactions due to a mutation of the arginin residue at position 5 of the βB strand in the SH2 domain.<ref name="Kousik"/> This suppression can lead to a non-functioning signalling pathway. | Several mutations in the SH2 domain can cause human diseases such as Noonan syndrome or basal cell carcinoma. For example, it can have a suppression of phosphotyrosine dependent interactions due to a mutation of the arginin residue at position 5 of the βB strand in the SH2 domain.<ref name="Kousik"/> This suppression can lead to a non-functioning signalling pathway. | ||
