Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain

Article Abstract:

The beta-1/beta-2 and beta-3/beta-4 loops of phospholipase C-delta pleckstrin homology domain (PLC-delta-PH) bind to inositol-1,4,5-trisphosphate (Ins(1,4,5)P3). Ins(1,4,5)P3 binds on the positively charged face of the electrostatically polarized domain. The binding involves hydrogen bonding and lysine side chain binding. The high affinity of PLC-delta-PH for Ins(1,4,5)P3 is due to the 1-phosphate group of Ins(1,4,5)P3. Mutations in two amino acids of the Burton's tyrosine kinase, counterparts of PLC-delta-PH residues that bind to Ins(1,4,5)P3, causes agammaglobulinemia.

Molecular structure, Phospholipases, Inositol phosphates

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PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface

Article Abstract:

Ligands containing the pleckstrin homology (PH) domain recruit signaling molecules to the cell surface. PH is a regulatory domain that controls phospholipase-C-delta-1 targeting to substrate-containing membranes and product inhibition of the enzyme. The phosphotyrosine-recognition domains (PTB), found in the signaling adapters Shc and IRS-1, contain the same domain. PTB domains bind to the phosphotyrosines in some activated receptor tyrosine kinases. Both PTB and PH domain ligands bring Shc and IRS-1 close to the membrane surface.

Physiological aspects, Ligands (Biochemistry), Amino acid sequence, Amino acid sequencing

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Nuclear signaling by receptor tyrosine kinases: The first robin of spring

Article Abstract:

A mechanism initiated by dual-protease signaling for the regulation of gene transcription and cell fate through direct nuclear signaling by an ErbB4 fragment is described. The findings demonstrate clearly that ErbB4 participates in a biologically significant signaling mechanism mediated by direct nuclear action of an activated ErbB4 fragment that is transported from the cell membrane to the nucleus in a manner that is regulated by a known ErbB4 ligand.

Science & research, Proteases, Cell membranes, Tyrosine

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