4933412E14Rik Activators

Zinc Pyrithione activates SH2 domain containing 7 by engaging in the JAK/STAT pathway, where it can enhance the phosphorylation of STAT proteins. Since SH2 domains bind to phosphorylated tyrosines on STAT proteins, the increased phosphorylation directly leads to the activation of SH2 domain containing 7 by increasing its substrate availability.

Genistein, a tyrosine kinase inhibitor, paradoxically activates SH2 domain containing 7 by inhibiting negative regulatory tyrosine kinases, which would otherwise prevent the activation of proteins within their signaling pathways. This inhibition allows for the activation of tyrosine-phosphorylated proteins that can interact with the SH2 domain, thus activating SH2 domain containing 7.

Sodium Orthovanadate acts as a phosphatase inhibitor and can activate SH2 domain containing 7 by preventing the dephosphorylation of proteins involved in its pathway. This sustained phosphorylation enhances the interaction of SH2 domain containing 7 with its binding partners, leading to its activation.

PMA activates protein kinase C (PKC), which can phosphorylate proteins that, once phosphorylated, may interact with SH2 domain containing 7, leading to its functional activation.

Insulin activates the insulin receptor and subsequent PI3K/Akt signaling pathway. Akt can phosphorylate downstream proteins that may serve as binding partners for SH2 domain containing 7, facilitating its activation.

Anisomycin activates the JNK pathway, leading to the phosphorylation of a wide array of proteins. Some of these phosphorylated proteins can serve as activators for SH2 domain containing 7 by providing appropriate binding sites for its SH2 domain.

SB 203580, while known as a p38 MAP kinase inhibitor, can activate SH2 domain containing 7 by altering the phosphorylation balance within the cell, potentially creating phosphorylated substrates that interact with and activate the SH2 domain of SH2 domain containing 7.

U0126 inhibits MEK, which indirectly leads to the activation of alternative pathways that can phosphorylate proteins, creating binding partners for the SH2 domain of SH2 domain containing 7, thus activating it.

LY294002 inhibits PI3K, leading to altered phosphorylation patterns within the cell. This alteration can result in the activation of compensatory signaling pathways that produce phosphorylated proteins capable of interacting with and activating SH2 domain containing 7.

Okadaic Acid is a serine/threonine phosphatase inhibitor that causes an increase in phosphorylated proteins within the cell, some of which may interact with SH2 domain containing 7, leading to its activation through increased substrate availability for its SH2 domain.