| Description | Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit [ ]. p110 is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. p85 is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are two inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are three inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110beta, and 3) p85 cSH2 domain with the kinase domain of p110beta [ ].Among all the class IA PI3K combinations, p85alpha/p110alpha heterodimer has been the most intensely investigated. p110alpha has been shown to be stabilized and inhibited by dimerization with p85alpha [ ]. Moreover, p85alpha (also called PIK3R1) has functions independent of its PI3K regulatory role. It can independently stimulate signalling pathways involved in cytoskeletal rearrangements []. PIK3R1 has been shown to play an important role in insulin signalling [].This entry represents the iSH2 domain found in PIK3R1. | Name | PIK3R1, inter-SH2 domain |
| Short Name | ISH2_PIK3R1 | Type | Domain |
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