Sandbox Reserved 1767: Difference between revisions

Line 28:

==RAF==

While RAF is not technically part of the SMP protein complex, it is crucial for advancement in the cell signaling pathway SMP helps mediate. RAF plays many different roles in this pathway and has many different domains. '''Figure 1''' shows RAF has a RAS binding domain (RBD), a N-terminal phosphorylated serine (NTpS), and a [https://www.~~jbc~~.~~org~~/~~article~~/~~S0021~~-~~9258~~(22)~~00689~~-~~5/fulltext~~. kinase domain] <ref name="Lavoie">PMID: 35970881</ref>. '''Figure 1''' shows these domains and mechanistically how RAF is involved in signal advancement or lack thereof. When its N-terminal serine is phosphorylated RAF is bound to a 14-3-3 protein dimer, inactivating the pathway. As shown in '''Figure 1''' the dephosphroylation of Ser259 starts the signaling cascade <ref name="Lavoie">PMID: 35970881</ref>.

While RAF is not technically part of the SMP protein complex, it is crucial for advancement in the cell signaling pathway SMP helps mediate. RAF plays many different roles in this pathway and has many different domains. '''Figure 1''' shows RAF has a RAS binding domain (RBD), a N-terminal phosphorylated serine (NTpS), and a [https://www.cell.com/fulltext/S0092-8674(00)81092-2. kinase domain] <ref name="Lavoie">PMID: 35970881</ref>. '''Figure 1''' shows these domains and mechanistically how RAF is involved in signal advancement or lack thereof. When its N-terminal serine is phosphorylated RAF is bound to a 14-3-3 protein dimer, inactivating the pathway. As shown in '''Figure 1''' the dephosphroylation of Ser259 starts the signaling cascade <ref name="Lavoie">PMID: 35970881</ref>.

==RAS==

Sandbox Reserved 1767: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 28: / Line 28: @@
 ==RAF==
-While RAF is not technically part of the SMP protein complex, it is crucial for advancement in the cell signaling pathway SMP helps mediate. RAF plays many different roles in this pathway and has many different domains. '''Figure 1''' shows RAF has a RAS binding domain (RBD), a N-terminal phosphorylated serine (NTpS), and a [https://www.jbc.org/article/S0021-9258(22)00689-5/fulltext. kinase domain] <ref name="Lavoie">PMID: 35970881</ref>. '''Figure 1''' shows these domains and mechanistically how RAF is involved in signal advancement or lack thereof. When its N-terminal serine is phosphorylated RAF is bound to a 14-3-3 protein dimer, inactivating the pathway. As shown in '''Figure 1''' the dephosphroylation of Ser259 starts the signaling cascade <ref name="Lavoie">PMID: 35970881</ref>.
+While RAF is not technically part of the SMP protein complex, it is crucial for advancement in the cell signaling pathway SMP helps mediate. RAF plays many different roles in this pathway and has many different domains. '''Figure 1''' shows RAF has a RAS binding domain (RBD), a N-terminal phosphorylated serine (NTpS), and a [https://www.cell.com/fulltext/S0092-8674(00)81092-2. kinase domain] <ref name="Lavoie">PMID: 35970881</ref>. '''Figure 1''' shows these domains and mechanistically how RAF is involved in signal advancement or lack thereof. When its N-terminal serine is phosphorylated RAF is bound to a 14-3-3 protein dimer, inactivating the pathway. As shown in '''Figure 1''' the dephosphroylation of Ser259 starts the signaling cascade <ref name="Lavoie">PMID: 35970881</ref>.
 ==RAS==