High impact information on PHIP

• In contrast to full-length PHIP, overexpression of the PH-binding region of PHIP has a pronounced inhibitory effect on insulin-induced IRS-1 tyrosine phosphorylation levels [1].
• Anti-phosphotyrosine immunoblots of PHIP revealed no discernible insulin receptor-regulated phosphorylation, suggesting that PHIP is not itself a substrate of the insulin receptor [1].
• The Au(I) complex 3 was found to exhibit intense blue-green, room-temperature phosphorescence (Phip = 0.06 and tauT = 22.7 micros) originating in the locally excited triplet of the phenanthrene moiety (3LE) in degassed 2-methyltetrahydrofuran solution [2].
• The inter-residual dihedral angles phi and phip of chitin and chitosan oligomers were determined from experimental 3J(C-H) constants and ROESY cross peaks [3].

Physical interactions of PHIP

• Importantly, mutants of the IRS-1 PH domain that disrupt the PH fold fail to bind to PHIP [1].

Other interactions of PHIP

• Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein [1].

References