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Mauricio Carvalho - May 11, 2023 - Other - short code - 427 views - 0 Comments - 0 Likes - 0 Reviews
Plexins are a family of transmembrane receptors that play important roles in various cellular processes, including cell migration, axon guidance, and cell-cell interactions. The plexin family consists of nine members (PlexinA1-4, PlexinB1-3, PlexinC1-2), each of which contains several domains that mediate different functions. One interesting aspect of plexins is their short code, which refers to the conserved sequence motif found in their cytoplasmic domain. In this article, we will delve into the significance of the plexin short code and its role in plexin signaling.
The plexin short code is a conserved sequence motif of about 30 amino acids that is located in the cytoplasmic domain of all plexins. The short code consists of two parts: a proline-rich motif (PRM) and a conserved tyrosine residue (Y). The PRM is thought to interact with SH3 domain-containing proteins, while the tyrosine residue serves as a phosphorylation site for intracellular signaling.
The plexin short code plays a crucial role in plexin signaling. The PRM interacts with various SH3 domain-containing proteins, including the adaptor protein Nck, which is involved in actin cytoskeleton remodeling. The tyrosine residue is phosphorylated by various kinases, including the Fes/Fer family of kinases, which activate downstream signaling pathways. The plexin short code also mediates the interaction between plexins and other signaling molecules, including Rho GTPases and semaphorins.
In conclusion, the plexin short code is a conserved sequence motif found in the cytoplasmic domain of all plexins. The short code consists of a proline-rich motif and a conserved tyrosine residue and plays a crucial role in plexin signaling by interacting with various SH3 domain-containing proteins and activating downstream signaling pathways. Understanding the significance of the plexin short code is important for elucidating the complex mechanisms underlying plexin signaling.