Showing papers on "Signal transducing adaptor protein published in 1989"
Journal Article•
TL;DR: A unique feature of HS1 suggests that the protein may be involved in signal transduction and regulation of gene expression, and the protein retains unique repeating motifs that shows a significant homology with the helix-turn-helix DNA-binding motif of several proteins reported previously.
Abstract: A novel cDNA clone designated as HS1, which show an expression pattern limited to human hematopoietic cells, was isolated. About 2kb mRNA of the clone was accumulated in all the mature and immature lymphoid and myeloid cell lines tested, and two of three erythroblastoid cell lines, but not in any cell lines of non-hematopoietic tissues. The same mRNA was also detected in normal lymphoid and myeloid tissues and peripheral blood lymphocytes, granulocytes and macrophages, but again not in non-hematopoietic tissues. Nucleotide sequence of the HS1 predicts a protein of 486 amino acids (Mr 53,931). N-terminal half of the protein retains unique repeating motifs, each of which shows a significant homology with the helix-turn-helix DNA-binding motif of several proteins reported previously. C-terminal half of the protein retains a region conserved between non-receptor tyrosine kinases (src family), phospholipase C(PLC)-148 and the crk oncogene product. A unique feature of HS1 suggests that the protein may be involved in signal transduction and regulation of gene expression.
146 citations
TL;DR: The results support the conjecture that the beta-type subunits (beta and beta') of the HA2 and HA2 adaptor complexes serve to attach the HA-2 adaptors to clathrin, while the other subunits may determine the specificity of binding to docking proteins and receptors on cytoplasmic membrane surfaces.
116 citations
16 citations
15 citations
01 Jan 1989
TL;DR: While many of the early events that occur immediately after receptor occupancy and lead to the activation of PKC are relatively well understood, the events which occur after PKC stimulation, which are responsible for the long term effects on cellular physiology, are still rather nebulous.
Abstract: The family of protein kinases known collectively as protein kinase C (PKC) occupies a central role in cellular signal transduction (Nishizuka, 1984; 1988). PKCs are associated with the cell surface membrane and are activated by diacylglycerols released as a result of increased phosphoinositol turnover occurring after stimulation of various cell surface receptors (Nishizuka, 1984; Berridge, 1985). In addition to these physiological activators, PKCs are potently stimulated by tumor promoting phorbol esters such as 12-0-tetradecanoyl-phorbol-13-acetate (TPA). While many of the early events that occur immediately after receptor occupancy and lead to the activation of PKC are relatively well understood, the events that occur after PKC stimulation, which are responsible for the long term effects on cellular physiology, are still rather nebulous.