Disease relevance of Baiap2

• In addition, the density and size of spines are decreased by a dominant-negative IRSp53 with a point mutation in the Src homology 3 (SH3) domain and a dominant-negative proline-rich region of WAVE2 (Wiskott-Aldrich syndrome protein family Verprolin-homologous protein), a downstream effector of IRSp53 that binds to the SH3 domain of IRSp53 [1].

High impact information on Baiap2

• Finally, IRSp53 depletion from cells prevents Tiam1-dependent lamellipodia induced by Tiam1 overexpression or platelet-derived growth factor stimulation [2].
• Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation [2].
• ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53 [3].
• Co-immunoprecipitation of IRSp53 and ProSAP2 solubilized from rat brain membranes indicates that the interaction occurs in vivo [3].
• Distinctive tissue distribution and phosphorylation of IRSp53 isoforms [4].

Biological context of Baiap2

• Isoforms of human IRSp53 have been reported, each with a unique amino acid sequence at the C-terminal end [4].

Anatomical context of Baiap2

• We have isolated rat and mouse cDNA clones for IRSp53 and determined expression patterns in rat central nervous system [5].
• An insulin-receptor substrate of 53-kDa protein (IRSp53) is an adapter protein, which interacts with the Rho-family of GTPases and mediates neurite outgrowth [4].
• IRSp53 hybridization signals were also detected in the cerebellum, subthalamic nucleus, pons, amygdala and hypothalamus [5].
• In situ hybridization analysis revealed enriched IRSp53 mRNA expression in rat forebrain structures, including the cerebral cortex (layers II/III, V and VI), striatum, hippocampus and olfactory bulb [5].
• Overexpression of IRSp53 in cultured neurons increases the density of dendritic spines but does not affect their length or width [1].

Associations of Baiap2 with chemical compounds

• Pharmacological profiles showed that a PKC inhibitor, but not other kinase inhibitors, specifically suppressed the synaptic translocation of IRSp53 in response to NMDA, and the selective activation of PKC with phorbol ester markedly induced the synaptic translocation [6].

References