C-JUN: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Andrew Rebeyka, David Canner, Michal Harel, Alexander Berchansky

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 == Protein Regulation ==
-C-Jun's ability to
+Changes made in the phosphorylation state of specific amino acids is one means by which c-Jun regulates transcription <ref name="ref6"/> PMID:8165146 </ref>.  To date two seperate sites of phosphorylation have been identified.  at the N-terminal end are the amino acids Ser63 and Ser73, which are phosphorylated in response to ''ras'' expression.  When ''ras'' is expressed, and Ser63 and Ser73 are phosphorylated, transcriptional activity of c-Jun increases.  the second site is located at the C-terminal which is very close in proximity to the DNA binding domain.  Here the residues are Thr214, Ser226, and Ser 232 <ref name="ref6"/>.  Unlike the two serines at the N-terminal end, phosphorylation at the C-terminal end inhibits DNA binding to c-Jun <ref name="ref6"/>.  therefore with the expression of such oncogenes as ''ras'' lead to dephsphorylation of these three residues.
+== Psychological Influences ==
-== OTHER ==
 The stress-induced signalling cascade may also active c-Jun by phosphorylation.  the N-ternminal protein kinase phosphorylates Ser63 and Ser73 <ref name="ref5"/> PMID:10064599 </ref> .  Another mechanism for the activation however is interestingly through intracellular calcium concentrations.  increasing these concentrations by opening the L-type voltage gated calcium channels
 It was found that the N-terminus contains both calcium and stress-regulated transcriptional activation domains <ref name="ref5"/>.  According to the study,distinct mechanisms of c-Jun control function by calcium and stress signals <ref name="ref5"/>.