Recruitment of PI3K to plasma membrane

Stable Identifier
Reaction [binding]
Homo sapiens
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In response to the TCR stimulation, phsophoinositides are phosphorylated on the 3-position of the inositol ring by PI3K to generate lipid second messengers that serve as membrane docking sites for a variety of downstream effector proteins such as PDK1 and PKB. PI3K is a heterodimer comprising a regulatory subunit p85 and a catalytic subunit p110 which associate constitutively and are activated upon interaction with tyrosine-phosphorylated proteins at the plasma membrane. The p85 subunit contains two SH2 domains and an SH3 domain. p85 subunit is involved in interaction with two phsophotyrosine residues of the adaptor protein TRIM with its two SH2 domains. This interaction is important in recruiting the p110 subunit to the plasma membrane and activate the p110 kinase activity, which is normally inhibited in the p85-p110 complex.
Literature References
PubMed ID Title Journal Year
16612002 Normal T-cell development and immune functions in TRIM-deficient mice

Lindquist, JA, Bruyns, E, Reinhold, D, Pfeffer, K, Kolsch, U, Kliche, S, Simeoni, L, Arndt, B, Schraven, B, Juling, N

Mol Cell Biol 2006
9687533 T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane

Mann, M, Shevchenko, A, Bruyns, E, Sagolla, K, Kirchgessner, H, Marie-Cardine, A, Schraven, B, Bensussan, A, Autschbach, F, Meuer, S

J Exp Med 1998
12660731 The role of PI3K in immune cells

Koyasu, S

Nat Immunol 2003
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