INOSITOL PHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C - COMPLETE CDNA AND PROTEIN SEQUENCES AND SEQUENCE HOMOLOGY TO TYROSINE KINASE-RELATED ONCOGENE PRODUCTS
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- INOSITOL PHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C - COMPLETE CDNA AND PROTEIN SEQUENCES AND SEQUENCE HOMOLOGY TO TYROSINE KINASE-RELATED ONCOGENE PRODUCTS
- Suh, Pann-Ghill; Ryu, Sung Ho; Moon, Kyung Ho; Suh, Hae Won; Rhee, Sue Goo
- Issue Date
- NATL ACAD SCIENCES
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.85, no.15, pp.5419 - 5423
- Antibodies against an inositol phospholipid-specific phospholipase C purified from bovine brain were used to screen rat brain λgt11 expression cDNA libraries. Complete sequences of three cDNA inserts yielded a cumulative sequence of 5106 base pairs. The deduced protein had 1289 amino acids with a calculated molecular weight of 148,431. The determination of an open reading frame was aided by the amino acid sequences of 21 tryptic peptides isolated from bovine brain phospholipase C. Only 9 residues of a total of 140 amino acid residues determined for the bovine enzyme were different from those deduced from the rat cDNA. Two regions of phospholipase C (amino acid residues 555-598 and 668-705) exhibited significant amino acid similarities to the products of various tyrosine kinase-related oncogenes (yes, src, fgr, abl, fps, fes, and tck). The homologous domain was located in the region that is not essential for the protein-tyrosine kinase activity but is likely to be involved in an interaction with cellular components that modulate kinase function. Therefore, this unexpected similarity raises the possibility that the 148-kDa phospholipase C and cytoplasmic tyrosine kinases are modulated by common cellular component(s).
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